Main stages of immunoassay methods evolutionary development
- DOI
- 10.5922/ATB-2025-1-2-1
- Pages
- 7-30
Abstract
The evolutionary pathway of diagnostic testing methods can be traced through the historical development and refinement of analytical tools. These tools are designed to identify sources, decipher mechanisms, and control processes inseparable from functional and morphological organization of living organisms under both normal and pathological conditions. In essence, this pathway represents a shift from subjective observation to objective formalization. The importance of this transition has been long recognized and is difficult to overestimate, as illustrated by the consequences of reckless human interference with nature. Furthermore, analysis of the global diagnostic systems market indicates significant growth: valued at USD 14.51 billion in 2021, it is forecast to reach USD 25.88 billion by 2029 (Data Bridge Market Research). The diversity of approaches to developing immunodiagnostic methods, as well as to biomedical analytics in general, is vast. Researchers continue to generate new methodologies. Accordingly, this review analyzes the evolutionary pathways of immunoassay techniques and tools that are actively applied in both laboratory and point-of-care testing.
Reference
1. Harma H. Particle technologies in diagnostics. National Technology Agency. Technolgy Review. Helsinki. 2002, 126, 1—30.
2. Widal F. On the sero-diagnosis of Thiphoid fever. The Lancet. 1896, 148(3820), 1371— 1372, DOI: 10.1016/s0140-6736(01)76589-0.
3. Wassermann A., Neisser A., Bruck C. Eine serodiagnostische Reaktion bei Syphilis. Deutsche medicinische Wochenschrift: Berlin. 1906, 32, 745—746.
4. Landsteiner K., Thomas C. C. The Specificity of Serological Reactions. 1936.
5. Heidelberger M. Quantitative absolute methods in the study of antigen-antibody reactions. Bacteriol. Rev. 1939, 3(1), 49—95, DOI: 10.1128/br.3.1.49-95.1939.
6. Kraus R. Ueber spezifische Reaktionen in keimfreien Filtraten aus Cholera-Typhus-Pestbouillonculturen erzeugt durch homologes Serum. [On specific reactions in germ-free filtrates from cholera- typhoid- plague- broth cultures produced by homologous serum]. Published in Wiener klinische Wochenschrift. 1897, 10, 32, 760—763, DOI: 10.3390/toxins16010033.
7. Ehrlich P. The Croonian lecture: On immunity. Proc. R. Soc. Lond. 1900, 66, 424.
8. Marrack J. R. The Chemistry of Antigens and Antibodies. Medical Research Council, Special Report Series. 1938, 230, 194.
9. Oudin J. L’analyse immunochimique du sérum de cheval par précipitation spécifique en milieu gélifié; premiers résultats [Immunochemical analysis of horse serum by specific precipitation in gelified medium; first results]. Bull. Soc. Chim. Biol. (Paris). 1947, 29(1—3), 140—149.
10. Elek S. D. Rapid identification of Proteus. J. Pathol. Bacteriol. 1948, 60(2), 183—192, DOI: 10.1002/path.1700600204.
11. Ouchterlony O. Air-borne infections; infection and spreading of infection in diphtheria with special reference to isolation wards. Acta Med. Scand. 1949, 134(4), 296—309.
12. Grabar P., Williams C. A. Method permitting the combined study of the electrophoretic and the immunochemical properties of protein mixtures; application to blood serum. Biochim. Biophys. Acta. 1953, 10(1), 93—94, DOI: 10.1016/0006-3002(53)90233-9.
13. Mancini G., Carbonara A. O., Heremans J. F. Immunochemical quantitation of antigens by single radial immunodiffusion. Immunochemistry. 1965, 2(3), 235—254, DOI: 10.1016/0019-2791(65)90004-2.
14. Laurell C. B. Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodies. Anal. Biochem. 1966, 15(1), 45—52, DOI: 10.1016/0003-2697(66)90246-6.
15. Coombs R. R. A., Mourant A. E., Race R. R. A new test for the detection of weak and incomplete Rh agglutinins. Br. J. Exp. Pathol. 1945, 26(4), 255—266.
16. Gupta S. K., Talwar G. P. Monoclonal antibodies based sandwich erythro-immunoassay and ’dot’ enzyme immunoassay for human chorionic gonadotropin in urine. Scand. J. Clin. Lab. Invest. 1986, 46(8), 751—759, DOI: 10.3109/00365518609084047.
17. Gupta S. K., Guesdon J. L., Avrameas S., Talwar G. P. Sandwich enzyme immunoassay of human chorionic gonadotropin using polystyrene beads as solid support. Ann. Inst. Pasteur Immunol. 1985, 136D(1), 47—55, DOI: 10.1016/s0769-2625(85)80074-x.
18. Bravo Oliva J. Rapid agglutination test on microscope slides in routine serological diagnosis. Med. Cir. Guerra. 1959, 21(3—4), 159—170.
19. Crosignant P. G., Polvani F., Surace M. Immunological assay of human chorionic gonadotrophin using HCG-coupled red cells agglutination. Folia Endocrinol. 1963, 16, 650—663.
20. Maurice Y., Provost A. Hemagglutination and hemagglutination inhibition tests with horse sickness virus. Limits of their interpretation. Rev. Elev. Med. Vet. Pays Trop. 1966, 19(4), 439—450.
21. Adler F. L., Liu C. T. Detection of morphine by gemagglutination-inhibition. J. Immunol. 1971, 106, 1684—1685.
22. Dierks R. E., Gough P. M. Passive haemagglutination test for rabies antibodies. Monogr. Ser. World Health Organ. 1973, 23, 147—150.
23. Van Doorn H. R., Hofwegen H., Koelewijn R., Gilis H., Wentink-Bonnema E., Pinelli E., et al. Reliable serodiagnosis of imported cystic echinococcosis with a commercial indirect hemagglutination assay. Diagn. Microbiol. Infect. Dis. 2007, 57(4), 409—412, DOI: 10.1016/j.diagmicrobio.2006.10.002.
24. Coombs R. R. A. Assay utilizing red cells as markers. In: Immunoassay for 80’s. Ed. A. Voller. MTP Press, Lancaster. 1981, 17—34.
25. Coombs R. R. A., Munro A. J. Storage-stable antibody-linked eritrocytes. Pat. 2138132. 1984.
26. Guesdon J. L., Avrameas S. Sensitive titration of antibodies and antigen using eritro-immunoassay. Ann. Immunol. 1980, 131, 3, 389—396.
27. Berson S. A., Yallow R. S. Insulin antagonists, insulin antibodies and insulin resistance. J. Med. 1958, 25(2), 155—159, DOI: 10.1016/0002-9343(58)90022-6.
28. Ekins R. P. Radioimmunoassay and saturation analysis. Basic principles and theory. Br. Med. Bull. 1974, 30(1), 3—11, DOI: 10.1093/oxfordjournals.bmb.a071163.
29. Teale J. D. Radioimmunoassay. 2 Scientific Foundations of Clinical Biochemistry. Chapter 19. Heinemann Medical. 1978, 279.
30. Erlanger B. F., Borek F., Beiser S. M., Lieberman S. Steroid-protein conjugates. I. Preparation and characterization of conjugates of bovine serum albumin with testosterone and with cortisone. J. Biol. Chem. 1957, 228(2), 713—727.
31. Byrnes D. J., Henderson L., Borody T., Rehfeld J. F. Radioimmunoassay of cholecystokinin in human plasma. Clin. Chim. Acta. 1981, 19, 111(1), 81—89, DOI: 10.1016/0009-8981(81)90424-1.
32. Wide L., Bennich H., Johansson S. G. Diagnosis of allergy by an in-vitro test for allergen antibodies. Lancet. 1967, 2, 1105—1107, DOI: 10.1016/s0140-6736(67)90615-0.
33. Engvall E., Perlmann P. Enzyme-linked immunosorbent assay (ELISA). Quantitative assay of immunoglobulin G. Immunochemistry. 1971, 8, 9, 871—874, DOI: 10.1016/0019-2791(71)90454-x.
34. Engvall E., Jansson K., Perlmann P. ELISA. Quantitative assay of protein antigen, IgG by means of enzyme — labelled antigen and antibody coated tubes. Biochem. Biophys. Acta. 1971, 251, 427—434, DOI: 10.1016/0005-2795(71)90132-2.
35. Engvall E., Perlmann P. Enzyme — linked immunosorbent assay (ELISA). Quantitation of specific antibodies by enzyme-labelled anti-immunoglobuline in antigen coated tubes. J. Immunol. 1972, 109, 129—135.
36. Engvall E. Enzyme-linked immunosorbent assay (ELISA). Biomedical applications of immobilized enzymes and proteins. Ed.: T. M. S. Chang. Plenum Press: N. Y. 1977, 2, 87—96.
37. Van Weemen B. K., Schuurs A. H.W.M. Immunoassay using antigen-enzyme conjugate. FEBS Lett. 1971, 15, 232—236, DOI: 10.1016/0014-5793(71)80319-8.
38. Rubinstein K. E., Schneider R. S., Ullman E. F. “Homogeneous” enzyme immunoassay. A new immunochemical technique. Biochem. Biophys. Res. Commun. 1972, 47, 846—851, DOI: 10.1016/0006-291X(72)90570-0.
39. Avrameas S., Uriel J. Méthode de marquage d’antigènes et d’anticorps avec des enzymes et son application en immunodiffusion [Method of antigen and antibody labelling with enzymes and its immunodiffusion application]. C. R. Acad. Hebd. Seances Acad. Sci. D. 1966, 262(24), 2543—2545.
40. Nakane P. K., Pierce G. B. Enzyme-Labelled antibodies preparation and application for the localization of antigen. J. Histochem. Cytochem. 1966, 14, 929, DOI: 10.1083/jcb.33.2.307.
41. Lam S. K., Devine P. L. Evaluation of capture ELISA and rapid immunochromatographic test for the determination of IgM and IgG antibodies produced during dengue infection. Clin. Diagn. Virol. 1998, 10(1), 75—81, DOI: 10.1016/s0928-0197(98)00002-6.
42. Dutaud D., Aubry L., Henry L., Levieux D., Hendil K. B., Kuehn L., et al. Ouali Development and evaluation of a sandwich ELISA for quantification of the 20S proteasome in human plasma. J. Immunol. Methods. 2002, 260(1—2), 183—193, DOI: 10.1016/s0022-1759(01)00555-5.
43. Pare J., Simard C. Comparison of commercial enzyme-linked immunosorbent assays and agar gel immunodiffusion tests for the serodiagnosis of equine infectious anemia. Can. J. Vet. Res. 2004, 68(4), 254—258.
44. Desai N., Filipovits J., Goldfarb J. Secretion of soluble HLA-G by day 3 human embryos associated with higher pregnancy and implantation rates: assay of culture media using a new ELISA kit. Reprod. Biomed. Online. 2006, 13(2), 272—277, DOI: 10.1016/s1472-6483(10)60626-8.
45. Ebinuma H., Miida T., Yamauchi T., Hada Y., Hara K., Kubota N., et al. Improved ELISA for Selective Measurement of Adiponectin Multimers and Identification of Adiponectin in Human Cerebrospinal Fluid. Clin. Chem. 2007, 53(8), 1541—1544, DOI: 10.1373/clinchem.2007.085654.
46. Tsao Z. J., Liao Y. C., Liu B. H., Su C. C., Yu F. Y. Development of a Monoclonal Antibody against Domoic Acid and Its Application in Enzyme-Linked Immunosorbent Assay and Colloidal Gold Immunostrip. J. Agric. Food Chem. 2007, 55(13), 4921—4927, DOI: 10.1021/jf0708140.
47. Coons A. H., Kaplan M. H. Localization of antigen in tissue cells; improvements in a method for the detection of antigen by means of fluorescent antibody. J. Exp. Med. 1950, 91(1), 1—13, DOI: 10.1084/jem.91.1.1.
48. Frank D. S., Sundberg M. W. Fluorescent labels comprising rare earth chelates. US Patent 4283382A. 1978.
49. Lovgren T., Heinonen P., Lehtinen P., Hakala H., Heinola J., Harju R., et al. Sensitive bioaffinity assays with individual microparticles and time-resolved fluorometry. Clin. Chem. 1997, 10, 1937—1943.
50. Chan W. C. W., Nie S. Quantum dot bioconjugates for ultrasensitive nonisotopic detection. Science. 1998, 281, 2016—2018, DOI: 10.1126/science.281.5385.2016.
51. Arai R., Ueda H., Tsumoto K., Mahoney W. C., Kumagai L., Nagamune T. Fluorolabeling of antibody variable domains with green fluorescent protein variants: application to an energy transfer-based homogeneous immunoassay. Protein Eng. 2000, 13, 369—376, DOI: 10.1093/protein/13.5.369.
52. Thorpe G. H., Williams L. A., Kricka L. J., Whitehead T. P., Evans H., Stanworth D. R. A rapid luminescently monitored enzyme immunoassay for Ig E. J. Immunol. Methods. 1985, 79(1), 57—63, DOI: 10.1016/0022-1759(85)90391-6.
53. Khadzhiolov A. I. Analysis of luminescence of tissue and fluids in the human and animal organism. Izv. Meditsinskite Inst. Bulg. Akad. Naukite Sofia Otd. Biol. Meditsinski Nauki. 1951, 1, 33—64.
54. Akimoto K., Shinmen Y., Sumida M., Asami S., Amachi T., Yoshizumi H., et al. Luminol chemiluminescence reaction catalyzed by a microbial peroxidase. Anal. Biochem. 1990, 189(2), 182—185, DOI: 10.1016/0003-2697(90)90104-h.
55. Terashima T., Okochi N., Kanno M., Satomi S., Taguchi Y., Mori S., et al. Measurement of the chemiluminescence from rat hepatocytes on reperfusion injury: preliminary report. Nippon Geka Gakkai Zasshi. 1992, 93(8), 869.
56. Fulwyler M. J. Optical chamber with spherical reflective portion and apparatus employing same. UK patent 1561042. 1976.
57. Herzenberg L. A., Sweet R. G. Fluorescence-activated cell sorting. Sci. Am. 1976, 234(3), 108—117.
58. Cook L., Irving D. Microsphere-based flow cytometric assays. J. Clin. Immunoassay. 1989, 12, 36—39.
59. Frengen J., Schmid R., Kierulf B., Nustad K., Paus E., Berge A., et al. Homogenous immunofluorometric assays of α-fetoprotein with macroporous, monosized particles and flow cytometry. Clin. Chem. 1993, 39, 2174—2181.
60. McHugh T. M. Flow microsphere immunoassay for the quantitative and simultaneous detection of multiple soluble analytes. Methods Cell Biol. 1994, 42, 575—595, DOI: 10.1016/s0091-679x(08)61096-1.
61. Soukka T., Paukkunen J., Härmä H., Lönnberg S., Lindroos H., Lövgren T. Supersensitive time-resolved immunofluorometric assay of free prostate-specific antigen with nanoparticle label technology. Clin. Chem. 2001, 47, 1269—1278.
62. Kruth H. S. Flow cytometry: rapid biochemical analysis of single cells. Anal. Biochem. 1982, 125(2), 225—242, DOI: 10.1016/0003-2697(82)90001-x.
63. Wan Dilla M. A., Dean P. H., Waerum O. D., Melamed M. R. Flow Cytometry: Instrumentation and Data Analysis. Academic Press: New York. 1985.
64. Jensen B. D., Horan P. K. Flow cytometry: rapid isolation and analysis of single cells. Meth. Enzymol. 1989, 171, 549—581, DOI: 10.1016/S0076-6879(89)71030-2.
65. Nolan J. P., Sklar L. A. The emergence of flow cytometry for sensitive, real-time measurements of molecular interactions. Nat. Biotechnol. 1998, 16(7), 633—638, DOI: 10.1038/nbt0798-633.
66. Edwards B. S., Oprea T., Prossnitz E. R., Sklar L. A. Flow cytometry for high-throughput, high-content screening. Curr. Opin. Chem. Biol. 2004, 8(4), 392—398, DOI: 10.1016/j.cbpa.2004.06.007.
67. Simons P. C., Shi M., Foutz T., Cimino D. F., Lewis J., Buranda T., et al. Ligand-receptor-G-protein molecular assemblies on beads for mechanistic studies and screening by flow cytometry. Mol. Pharmacol. 2003, 64(5), 1227—1238, DOI: 10.1124/mol.64.5.1227.
68. Waller A., Simons P., Prossnitz E. R., Edwards B. S., Sklar L. A. High throughput screening of G-protein coupled receptors via flow cytometry. Comb. Chem. High Throughput Screen. 2003, 6(4), 389—397, DOI: 10.2174/138620703106298482.
69. Sklar L. A., Edwards B. S., Graves S. W., Nolan J. P., Prossnitz E. R. Flow cytometric analysis of ligand-receptor interactions and molecular assemblies. Annu. Rev. Biophys. Biomol. Struct. 2002, 31, 97—119, DOI: 10.1146/annurev.biophys.31.082901.134406.
70. Engler R., Judon C., Langlade J. P., Jayle M. F. An immunonephelometric determination of rabbit haptoglobin. Article in French. C. R. Acad. Hebd. Seances Acad. Sci. D. Sci Nat. 1975, 280(18), 2157—2159.
71. Van Munster P. J., Hoelen G. E., Samwel-Mantingh M., Holtman-Van Meurs M. A turbidimetric immuno assay (TIA) with automated individual blank compensation. Clin. Chim. Acta. 1977, 76(3), 377—388, DOI: 10.1016/0009-8981(77)90165-6.
72. Evans S. E. Rapid determination of alpha-fetoprotein in amniotic fluid using an automated immunoturbidimetric technique. Ann. Clin. Biochem. 1980, 17(3), 130—133, DOI: 10.1177/000456328001700305.
73. Kleine T. O., Merten B. Rapid manual immunoturbidimetric and immunonephelometric assays of prealbumin, albumin, IgG, IgA and IgM in cerebrospinal fluid. J. Clin. Chem. Clin. Biochem. 1980, 18(4), 245—254, DOI: 10.1515/cclm.1980.18.4.245.
74. Spencer K., Price C. P., Anthony F., Wood P. J. Kinetic immunoturbidimetry: the measurement of pregnancy specific beta 1glycoprotein. Clin. Chim. Acta. 1979, 99(2), 177—187, DOI: 10.1016/0009-8981(79)90041-x.
75. Boguslavski R. C., Li T. M. Homogeneous immunoassay. Appl. Biochem. Biotechnol. 1982, 7(5), 401—414.
76. Oellerich M. Enzyme-immunoassay: a review. J. Clin. Chem. Clin. Biochem. 1984, 22(12), 895—904.
77. Van Weemen B. K. ELISA: highlights of the present state of the art. J. Virol. Methods. 1985, 10(4), 371—378, DOI: 10.1016/0166-0934(85)90055-2.
78. Ekins R. P. Merits and disadvantages of different labels and methods of immunoassay. In: Immunoassay for the 80’s. MTP Press: Lancaster. 1981, 5—16.
79. Ekins R. P., Dacubu S. The development of high sensitivity pulsed light, time-resolved fluoroimmunoassay. Pure Appl. Chem. 1985, 57, 3, 473—482.
80. Shall R. F., Tenoso H. J. Alternatives to radioimmunoassay: labels and methods. Clin. Chem. 1981, 27, 7, 1157—1164.
81. Olsson T., Thore A. Chemiluminescence and its use in immunoassay. In: Immunoassay for the 80’s. MTP Press: Lancaster. 1981, 113—125.
82. Woodhead J. S., Weeks I. Chemiluminescence immunoassay. Pure and Appl. Chem. 1985, 57, 3, 523—529.
83. Fukada H., Haga A., Fujita T., Hiramatsu N., Sullivan C. V., Hara A. Development and validation of chemiluminescent immunoassay for vitellogenin in five salmonid species. Comp. Biochem. Physiol. Part A Mol. Integr. Physiol. 2001, 130(1), 163—170, DOI: 10.1016/s1095-6433(01)00381-6.
84. Lin J., Ju H. Electrochemical and chemiluminescent immunosensors for tumor markers. Biosens Bioelectron. 2005, 20(8), 1461—1470, DOI: 10.1016/j.bios.2004.05.008.
85. Liu Y. M., Mu H. B., Zheng Y. L., Wang C. Q., Chen Y. H., Li F. R., et al. Capillary electrophoretic immunoassay for alpha-fetoprotein with chemiluminescence detection. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 2007, 855, 2, 280—285, DOI: 10.1016/j.jchromb.2007.04.033.
86. Lindstedt G., Himmelmann C. E., Salsmans R., Valentin K. Home testing for pregnancy-can it be recommended? Scand. J. Clin. Lab. Invest. 1982, 42(4), 371—376.
87. Wang C. F., Gemzell C. Neocept: a simple, sensitive urine test of early pregnancy in women undergoing ovulation induction. J. Reprod. Med. 1982, 27(4), 193—195.
88. Nielsen M. S., Barton S. D., Hatasaka H. H., Stanford J. B. Comparison of several one-step home urinary luteinizing hormone detection test kits to OvuQuick. Fertil. Steril. 2001, 76(2), 384—387, DOI: 10.1016/s0015-0282(01)01881-7.
89. Anderton D. J., Gronow M., Kungdon C. F.M., Ghesman J. Tools for decentralized clinical biochemistry testing. Optimal use of the clinical laboratory. Karger: Basel. 1986, 129—136.
90. Jeffers J. G., Shanley K. J., Meyer E. K. Diagnostic testing of dogs for food hypersensitivity. J. Am. Vet. Med. Assoc. 1991, 198(2), 245—250.
91. Laing J. A., Heap R. B. The concentration of progesterone in milk of cows during the reproductive cycle. Br. Vet. J. 1971, 127(8), 19—22, DOI: 10.1016/s0007-1935(17)37432-8.
92. Sauer M. J., Foulkes J. A., Cookson A. D. Direct enzyme immunoassay of progesterone in bovine milk. Steroids, 1981, 38, 45—53, DOI: 10.1016/0039-128X(81)90020-9.
93. Davies J., Fletcher N. A. Evaluation of an enzyme immunoassay kit for the quantitative assessment of progesterone in buvine milk samples. Vet. Record. 1987, 1209110, 257—258, DOI: 10.1136/vr.120.11.257.
94. Saba N. J., Hatterslay J. P. Direct estimation of estrone sulphate in cow serum for a rapid pregnancy diagnosis test. J. Reprod. Fertil. 1981, 62, 87—92, DOI: 10.1530/jrf.0.0620087.
95. Hamon M., Fleet I. R., Holdsworth R. J., Heap R. B. The time of detection of estrone sulphate in milk and the diagnosis of pregnancy in cows. Br. Vet J. 1981, 137(1), 71—77, DOI: 10.1016/s0007-1935(17)31790-6.
96. Shen J. T. Gamma stick. US Patent 4135884A. 1979.
97. Al-Yousif Y., Anderson J., Chard-Bergstrom C., Bustamante A., Muenzenberger M., Austin K, et al. Evaluation of a latex agglutination kit (Virogen Rotatest) for detection of bovine rotavirus in fecal samples. Clin. Diagn. Lab. Immunol. 2001, 8(3), 496—498, DOI: 10.1128/CDLI.8.3.496-498.2001.
98. Al-Yousif Y., Anderson J., Chard-Bergstrom C., Kapil S. Development, evaluation, and application of lateral-flow immunoassay (immunochromatography) for detection of rotavirus in bovine fecal samples. Clin. Diagn. Lab. Immunol. 2002, 9(3), 723—724, DOI: 10.1128/CDLI.9.3.723-724.2002.
99. Heathcote J. G., Hillert J. R. Aflotoxins: Chemical and biological aspects. Development’s in Food science. Elsevier: Amsterdam. 1978, 1, 97—108.
100. Watanabe H., Satake A., Kido Y., Tsuji A. Monoclonal-based enzyme-linked immunosorbent assay and immunochromatographic assay for enrofloxacin in biological matrices. Analyst. 2002, 127(1), 98—103, DOI: 10.1039/B109427K.
101. Zhou P., Lu Y., Zhu J., Hong J., Li B., Zhou J., et al. Nanocolloidal gold-based immunoassay for the detection of the N-methylcarbamate pesticide carbofuran. J. Agric. Food Chem. 2004, 52(14), 4355—4359, DOI: 10.1021/jf0499121.
102. Zhang H., Meyerhoff M. Gold-coated Magnetic particles for solid-phase immunoassay: enhancing immobilized antibody binding efficiency and analytical performance. Anal. Chem. 2006, 78, 609—616, DOI: 10.1021/ac051720x.
103. Egger D., Bienz R. Colloidal gold staining and immunoprobing of proteins on the same nitrocellulose blot. Anal. Biochem. 1987, 166, 413—417, DOI: 10.1016/0003-2697(87)90592-6.
104. Kramarcy N. R., Sealock R. Commercial preparations of colloidal gold-antibody complex frequently contain free active antibody. J. Histochem. Cytochem. 1991, 39(1), 37—39, DOI: 10.1177/39.1.1983872.
105. Chakraborty U. R., Black N., Brooks H. G., Campbell C., Gluck K., Harmon F., et al. An immunogold assay system for the detection of antigen or antibody. Ann. Biol. Clin. 1990, 8, 403—408.
106. Martin J. M., Paques M., van der Velden-de Groot T. A., Beuvery E. C. Characterization of antibody labelled colloidal gold particles and their applicability in a sol particle immunoassay (SPIA). J. Immunoassay. 1990, 11(1), 31—47, DOI: 10.1080/01971529008053256.
107. Moeremans M., Daneels G., Van Dijck A., Langanger G., De Mey J. Sensitive visualization of antigen-antibody reactions in dot and blot immune overlay assay with immunogold and immunogold silver staining. J. Immunol. Meth. 1984, 74920, 353—360, DOI: 10.1016/0022-1759(84)90303-X.
108. Leuvering J. H., Thal P. J., van der Waart M., Schuurs A. H. Sol particle immunoassay (SPIA). J. Immunoassay. 1980, 1(1), 77—91, DOI: 10.1080/01971528008055777.
109. Leuvering J. H., Goverde B. C., Thal P. J., Schnurs A. H. A gomogeneous sol particle immunoassay for human chorionic gonadotrophin using monoclonal antibodies. J. Immunol. Meth. 1983, 60, 9—23, DOI: 10.1016/0022-1759(83)90330-7.
110. Zhang C., Zhang Y., S. Wang S. Development of multianalyte flow-through and lateral-flow assays using gold particles and horseradish peroxidase as tracers for the rapid determination of carbaryl and endosulfan in agricultural products. J. Agric. Food Chem. 2006, 54(7), 2502—2507, DOI: 10.1021/jf0531407.
111. Lee E. J., Kim Y., Lim J., Kim M., Kang C. S., Lee J. H., et al. Simple immunohistochemical staining method using large sized gold colloid conjugated secondary antibody. Ann. Clin. Lab. Sci. 2007, 37(2), 152—157.
112. Gamliel H., Polliack A. Scanning immunoelectron microscopy markers. Isr. J. Medl Sci. 1979, 15(8), 639—646.
113. Mannweiler K., Hohenberg H., Bohn W., Rutter G. Protein-A gold particles as markers in replica immunocytochemistry: high resolution electron microscope investigations of plasma membrane surfaces. J. Microsc. 1982, 126(Pt 2), 145—149, DOI: 10.1111/j.1365-2818.1982.tb00363.x.
114. De Waele M., De Mey J., Moeremans M., Broodtaerts L., Smet L., Van Camp B. Colloidal gold as a marker for the light microscope detection of leukocyte cell surface antigens with monoclonal antibodies. J. Clin. Immunol. 1982, 2(3 Suppl), 24S—31S.
115. Hutchison N. J., Langer-Safer P. R., Ward D. C., Hamkalo B. A. In situ hybridization at the electron microscope level: hybrid detection by autoradiography and colloidal gold. J. Cell Biol. 1982, 95(2 Pt 1), 609—618, DOI: 10.1083/jcb.95.2.609.
116. Romano E. L., Stolinsky C., Hughes-Jones C. An antiglobulin reagent labeled with colloidal gold for use in electron micriscipy. Immunochem. 1974, 11, 521—522, DOI: 10.1016/0019-2791(74)90162-1.
117. Roth J. The preparation of protein A-gold complexes with 3 nm and 15nm gold particles and their use in labelling multiple antigens on ultra-thin sections. Histochem J. 1982, 14(5), 791—801, DOI: 10.1007/BF01033628.
118. Horrisberger M., Rosset J. Colloidal gold, a useful marker for transmission and scanning electron microscopy. J. Histochem. Citochem. 1977, 25, 295—305, DOI: 10.1177/25.4.323352.
119. Horrisberger M., Vonlanthen M. Simultaneous localization of hepatic binding protein specific for galactose and of galactose-containing receptors on rat hepatocytes. J. Histochem. Cytochem. 1978, 26, 960—966, DOI: 10.1177/26.11.722052.
120. Frens J. A device for quantative measuring of shivering in goats. Lab. Anim. 1973, 7(3), 287—288, DOI: 10.1258/002367773780944003.
121. Slot J. W., Geuze H. J. Sizing of protein A-colloidal gold probes for imunoelectron microscopy. J. Cell Biology. 1981, 90(2), 533—536, DOI: 10.1083/jcb.90.2.533.
122. Van den Pol A. N. Colloidal gold and biotin-avedin conjugates as ultrasructural markers for neural antigens. Quartery J. of Experimental Physiology. 1984, 69, 1—33, DOI: 10.1113/expphysiol.1984.sp002771.
123. Litchfield W. J., Freytag J. W., Adamich M. Highly sensitive immunoassays based on use of liposomes without complement. Clin. Chem. 1984, 30(9), 1441—1445.
124. Rongen H. A., Bult A., van Bennekom W. P. Liposomes and immunoassays. J. Immunol. Methods. 1997, 204(2), 105—133, DOI: 10.1016/s0022-1759(97)00041-0.
125. Compbeli R. L., Wagner D. B., O’Connel J. P. Solid phase assay with visual readout. US Patent 4703017A. 1987.
126. Remington J. S., Eimstad W. M., Aranjo F. G. Detection of immunoglobulin M antibodies with antigen-tagged latex particles in an immunosorbent assay. J. Clin. Microbiol. 1983, 17(5), 939—941, DOI: 10.1128/jcm.17.5.939-941.1983.
127. Sakai Y., Hibino M. Distribution-Analyzing latex immunoassay (DALIA): methods for determination of antigen and for elimination of non-specific reaction induced by rheumatoid factor. Chem. Pharm. Bull. 1989, 37, 11, 3010—3014, DOI: 10.1248/cpb.37.3010.
128. Liu Y. C., Dong G. J., Zhao Y. C. Preparation of diazotzed polystyrene latex and its use in agglutination assays. J. Immunol. Meth. 1989, 124, 159—163, DOI: 10.1016/0022-1759(89)90348-7.
129. Gerber M. A., Caparas L. S., Randolph M. F. Evaluation of a new latex agglutination test for detection of streptolysin O antibodies. J. Clin. Microbiol. 1990, 28(3), 413—415, DOI: 10.1128/jcm.28.3.413-415.1990.
130. Reichwein B., Jungkind D., Guardiani M., Gilbert R., Prosswimmer G., Amadio P. Comparison of two rapid latex agglutination methods for detection of group A streptococcal pharyngitis. Am. J. Clin. Pathol. 1986, 86(4), 529—532, DOI: 10.1093/ajcp/86.4.529.
131. Fujikawa S., Ohkuni M. A new latex agglutination test for rapid diagnosis of group A streptococci. Jpn. Circ. J. 1986, 50(12), 1251—1252, DOI: 10.1253/jcj.50.1251.
132. Chang M. J., Mohla C. Ten-minute detection of group A streptococci in pediatric throat swabs. J. Clin. Microbiol. 1985, 21(2), 258—259, DOI: 10.1128/jcm.21.2.258-259.1985.
133. Hanlon J. T., Caiola S. M., Muhlbaier L. H., Dennis B. H., Edelman D. A., Dingfelder J. R. An evaluation of the sensitivity of five home pregnancy tests to known concentrations of human chorionic gonadotropin. Am. J. Obstet. Gynecol. 1982, 144(7), 778—782, DOI: 10.1016/0002-9378(82)90351-9.
134. Imai S., Kouda Y., Nishihara T., Kinoshita M. Immunochromatographic assay with improved colored latex. US Patent 5266497A. 1991.
135. Kojima T., Arai M., Sadamoto S., Ikedo M., Yui I. Evaluation of the diagnostic reagents which detect group A Streptococcus with the immunochromatographical method. Rinsho Biseibutshu Jinsoku Shindan Kenkyukai Shi. 2002, 12(2), 91—95.
136. Ehrlich T. P., Schwartz R. H., Wientzen R., Thorne M. M. Comparison of an immunochromatographic method for rapid identification of group A streptococcal antigen with culture method. Arch. Fam. Med. 1993, 2(8), 866—869, DOI: 10.1001/archfami.2.8.866.
137. Yatsyshina S. B., Kulichenko T. V., Artemova I. V., Rybalka O. V., Elkina M. N. Use of immunochromatographic tests in a laboratory diagnostic algoritm for influenza. Epidemiology and infectious diseases. Current issues. 2018, 1, 48.
138. Mitamura K., Yamazaki M., Ichikawa M, Kimura K., Kawakami C., Shimizu H., et al. Evaluation of an immunochromatography test using enzyme immunoassay for rapid detection of influenza A and B viruses. Kansenshogaku Zasshi. 2004, 78(7), 597—603, DOI: 10.11150/kansenshogakuzasshi1970.78.597.
139. May K. Home tests to monitor fertility. Am. J. Obstet. Gynecol. 1991, 165(6Pt2), 2000—2002, DOI: 10.1016/s0002-9378(11)90566-3.
140. Nielsen M. S., Barton S. D., Hatasaka H. H., Stanford J. B. Comparison of several one-step home urinary luteinizing hormone detection test kits to OvuQuick. Fertil. Steril. 2001, 76(2), 384—387, DOI: 10.1016/s0015-0282(01)01881-7.
141. Vartdal F., Gaudernack G., Funderud S., Bratlie A., Lea T., Ugelstad J., et al. HLA class I and II typing using cells positively selected from blood by immunomagnetic isolation--a fast and reliable technique. Tissue Antigens. 1986, 28(5), 301—312, DOI: 10.1111/j.1399-0039.1986.tb00500.x.
142. Lie O., Vartdal F., Funderud S., Gaudernack G., Olsaker I., Frеysadal E., et al. Immunomagnetic isolation of cells for serological BoLA typing. Anim. Genet. 1988, 19(2), 75—86.
143. Khramtsov P., Kropaneva M, Byzov I., Minin A., Mysik A., Timganova V., et al. Conjugation of carbon coated-iron nanoparticles with biomolecules for NMR-based assay. Colloids and Surfaces B: Biointerfaces. 2019, 176, 256—264, DOI: 10.1016/j.colsurfb.2019.01.009.
144. Khramtsov P., Barkina I., Kropaneva M., Bochkova M., Timganova V., Nechaev A., et al. Magnetic Nanoclasters Coated with Albumin, Casein and Gelatin: Size Tuning, Relaxivity, Stability, Protein Corona, and Application in Nuclear Magnetic Resonance Immunoassay. Nanomaterials. 2019, 9, 1345, DOI: 10.3390/nano9091345.
145. Khramtsov P., Kropaneva M., Bochkova M., Timganova V., Zamorina S., Rayev M. Solid-phase nuclear magnetic resonance immunoassay for the prostate-specific antigen by using protein-coated magnetic nanoparticles. Microchim. Acta. 2019, 186(12), 768, DOI: 10.1007/s00604-019-3925-4.
146. Khramtsov P., Kropaneva M., Bochkova M., Kiselkov D., Timganova V., Zamorina S., et al. Nuclear magnetic resonance immunoassay of tetanus antibodies based on the displacement of magnetic nanoparticles. Anal. Bioanal. Chem. 2021, 413(5), 1461—1471, DOI: 10.1007/s00216-020-03112-7.
147. Mitani K., Une H. Dyed inorganic composite particles bound with immunoreactive substances for use in microtiter tests. Europ. Pat. 250700A2. 07.01.88.
148. Nilsson K. G. I. Preparation of nanoparticles conjugated with enzyme and antibody and their use in heterogeneous enzyme immunoassay. J. Immunol. Meth. 1989, 122, 273—277, DOI: 10.1016/0022-1759(89)90274-3.
149. Wechers J. H., Van Es R. M., Keiser G. D., Van Doorn A. W. J., Van Gelder W. M. J. Stained sols of non-metallic elements or compounds, their preparaition and use. Europ. Pat. 89202883.8. 30.05.90.
150. Haun M., Wasi S. Biotinylated antibodies bound to streptavidin beads: a versatile solid matrix for immunoassays. Analyt. Biochem. 1990, 191, 337—342, DOI: 10.1016/0003-2697(90)90228-2.
151. Zelikman I., Hjerten S. Protein immunoassay based on agglutination of antibody-coated ferric oxide particles. J. Immunol. Meth. 1988, 114, 267—273, DOI: 10.1016/0022-1759(88)90183-4.
152. Hirschfeld T. Dye target reagent. US Patent 4166105. 28.08.1979.
153. Tarcha P. J., Wong M., Donovan J. J. Indicator reagents, diagnostic assays and kits employing organic polymer latex particles. Europ. Patent 89116594.6. 28.05.1990.
154. Russel J. C., Yang H., Yost D. A. Method for determinig sample analyte amount-involves reacting sample with colloidal non-metal particles before optical measurement of analyte-particle complexes. Europ. Patent 298368A. 11.01.89.
155. Spallholz J. E. Stable isotopic immunoassay method employing nonradioactive selenium label. US Patent 4341757A. 27.07.82.
156. Van Es R. M., Keiser G. D., Van Doorn A. W.J. Method for an increased visualisation of the reacthion product of a specifically binding substance and a corresponding bindable substance, and kit therefore. Europ. Patent 89202884.6. 23.05.90.
157. Wechers J. H., Van Es R. M., Keiser G. D., Van Doorn A. W. J., Van Gelder W. M. J. Stained sols of non-metallic elements or compounds, their preparaition and use. Europ. Patent 89202883.8. 30.05.90.
158. Yost D. A., Russel J. C., H. Yang H. Non-metal colloidal particle immunoassay. Europ. Patent 0298368A2. 11.01.89.
159. Gribnau Th. C. J., Roeles F., Leuvering J. H. W. The application of water-dispersible hydrophobic dyes as labels in immunoassays. Europ. Patent 80201241.9. 02.05.85.
160. Snowden K., Hommel M. Antigen detection immunoassay using dipsticks and colloidal dyes. J. Immunol. Meth. 1991, 140, 57—65, DOI: 10.1016/0022-1759(91)90126-Z.
161. Xie Y., Xue C., W. Lou W. Establishment and application of dipstick sandwich colloidal dye immunoassay for circulating antigen detection in schistosomiasis patients. Zhongguo Ji Sheng Chong Xue Yu Ji Sheng Chong Bing Za Zhi. 1999, 17(3), 129—131.
162. Xiang X., Tianping W., Zhigang T. Development of a rapid, sensitive, dye immunoassay for schistosomiasis diagnosis: a colloidal dye immunofiltration assay. J. Immunol. Methods. 2003, 280(1—2), 49—57, DOI: 10.1016/s0022-1759(03)00196-0.
163. Xiao X., Wang T., Ye H., Qiang G., Wei H., Tian Z. Field evaluation of a rapid, visually-read colloidal dye immunofiltration assay for Schistosoma japonicum for screening in areas of low transmission. Bull. World Health Organ. 2005, 83(7), 526—533.
164. Adamov A., Agafonov V. Suspension antigens, antibodies and immunosorbents. Medicine: Moscow. 1969.
165. Gribnau Th. C. J., Van Sommeren A., Van Dinther F. DIA-disperse dye immunoassay. Affinity Chromatogr. Biol. Recognit. Proc. Int. Symp. 1983, 5, 375—380.
166. Anderson R. R. A solid phase system incorporating tetrazolium salts for use in ligand-receptor assays. Europ. Patent 253578A2. 20.01.88.
167. Rounds D. E. Immunoassay utilizing formazan-prelabeled reactants. US Patent 4786589A. 22.11.88.
168. Szewczuk A., Kuropatwa M., Rapak A. The use of antibodies labelled with dyes for fast and simple assay of some human proteins by immunofiltration technique. Arch. Immunol. Ther. Exp. 1992, 40, 325—329.
169. Kang J., Youn B., Oh Y. H. Carbon black immunochemical label. US Patent 5252496A. 12.10.1993.
170. Van Doorn A. W. J. Immunodetermination using non-metallic labels. Europ. Patent 88202597.6. 21.06.89.
171. Rayev M. B., Ambrosov I. V., Briko N. I. A Novel Method for the Serodiagnosis of Group A Streptococcal Antibodies. Streptococci and the Host. Ad. Thea Horaud et al. Advances in Experimental medicine and biology. Plenum Press: New York and London. 1997, 418, 327—329.
172. Rayev M., Shmagel K. Carbon-protein covalent conjugates in noninstrumental immunodiagnostic systems. Journal of Immunological Methods. 2008, 336, 1, 9—15, DOI: 10.1016/j.jim.2008.03.005.
173. Khramtsov P., Bochkova M., Timganova V., Zamorina S., Rayev M. Dot immunoassay for the simultaneous determination of postvaccination immunity against pertussis, diphtheria, and tetanus. Anal. Bioanal. Chem. 2017, 409(15), 3831—3842, DOI:10.1007/s00216-017-0327-5.
174. Khramtsov P., Kropaneva M., Kalashnikova T., Bochkova M., Timganova V., Zamorina S., Rayev M. Highly stable conjugates of carbon nanoparticles with DNA aptamers. Langmuir. 2018, 34(35), 10321—10332, DOI: 10.1021/acs.langmuir.8b01255.
175. Kropaneva M., Khramtsov P., Bochkova M., Lazarev S., Kiselkov D., Rayev M. Vertical Flow Immunoassay Based on Carbon Black Nanoparticles for the Detection of IgG against SARS-CoV-2 Spike Protein in Human Serum: Proof-of-Concept. Biosensors. 2023, 13, 857, DOI: 10.3390/bios13090857.
176. Khramtsov P., Bochkova M., Timganova V., Zamorina S., Rayev M., Kiselkov D. Albumin nanoparticles loaded with hemin as peroxidase mimics for immunoassay. Chemistry Select. 2022, 7, 3, e202103892, DOI: 10.1002/slct.202103892.
177. Khramtsov P., Kropaneva M., Bochkova M., Zamorina S., Rayev M., Timganova V., et al. Prussian blue nanozymes with enhanced catalytic activity: size tuning and application in elisa-like immunoassay. Nanomaterials. 2022, 12, 10, 1630, DOI: 10.3390/nano12101630.
178. Khramtsov P, Kropaneva M, Bochkova M, Timganova V, Kiselkov D, Zamorina S, et al. Synthesis and Application of Albumin Nanoparticles Loaded with Prussian Blue Nanozymes. Colloids and Interfaces. 2022, 6(2), 29, DOI: 10.3390/colloids6020029.
179. Oh Y. K., Joung H. A., Kim S., Kim M. G. Vertical flow immunoassay (VFA) biosensor for a rapid one—step immunoassay. Electronic Supplementary Material (ESI) The Royal Society of Chemistry. Lab Chip. 2013, 13, 768—772, DOI: 10.1039/C2LC41016H.
180. Plaksin D., Rayev M., Gromakovskaya E. Method of stereospecific analysis and method of obtaining a conjugate for stereospecific analysis. Patent of the Russian Federation No.2089912 of 10.09.1997. Bulletin “Inventions”. 1997, 25, 336.