Montagne P, Laroche P, Cuilliere M L, Riochet D, Flecheux O, Varcin P, Marchand J, Pau B, Duheille J
Immunology Laboratory, Faculty of Medicine, Nancy, France.
J Immunoassay. 1991;12(2):165-83. doi: 10.1080/01971529108055065.
Polyfunctional hydrophilic microspheres (MS) can be produced by copolymerisation with gamma-irradiation of acrylic monomers. Transferrin (TRF) can be covalently bound to these MS by reaction between aldehyde groups of the MS and primary amino groups of the protein. MS-TRF conjugates thus obtained are agglutinated by specific antiserum and this agglutination is inhibited by free TRF. Agglutination and inhibition are quantified by measurement of the light scattered by MS-TRF conjugate clusters with a specially designed nephelometer, a process designated as microparticle enhanced nephelometric immunoassay (NEPHELIA (R)) for TRF. Recovery, correlation and reproducibility studies, simultaneously performed in three different laboratories, show that this TRF immunoassay is accurate for a large concentration range. NEPHELIA (R) may appear as an alternative method for a large variety of molecules.
多功能亲水性微球（MS）可通过丙烯酸单体的γ辐射共聚反应制备。转铁蛋白（TRF）可通过微球的醛基与蛋白质的伯氨基之间的反应共价结合到这些微球上。由此获得的MS-TRF缀合物可被特异性抗血清凝集，并且这种凝集可被游离的TRF抑制。通过使用专门设计的浊度计测量MS-TRF缀合物簇散射的光来定量凝集和抑制，该过程称为TRF的微粒增强浊度免疫分析（NEPHELIA（R））。在三个不同实验室同时进行的回收率、相关性和重现性研究表明，这种TRF免疫分析在很大的浓度范围内是准确的。NEPHELIA（R）可能是多种分子的替代方法。
