Study ofβ‐casein denaturation by microparticle‐enhanced nephelometric immunoassay
作者:
N.El bari,
P. Montagne,
M. L. Cuilliere,
G. Humbert,
G. Linden,
J. Duheille,
期刊:
Food and Agricultural Immunology
(Taylor Available online 1992)
卷期:
Volume 4,
issue 4
页码: 229-240
ISSN:0954-0105
年代: 1992
DOI:10.1080/09540109209354772
出版商: Taylor & Francis Group
关键词: ß‐casein;ß‐casein denaturation;ß‐casein peptides;immunonephelometry;particle immunoassay;plasmin activity
数据来源: Taylor
摘要:
Rabbit anti‐native bovine ß‐casein antiserum reacted with native ß‐casein and fragments f( 1–105/7) and f( 106–209) formed during ß‐casein proteolysis by plasmin. Agglutination of ß‐casein‐coated microparticles by anti‐native ß‐casein antiserum was weakly inhibited by ß‐casein f(1–105/7) and ß‐casein f( 106–209) (0·04 and 1·4%, respectively, compared with native ß‐casein). Immunoreactivity of these ß‐casein peptides in microparticle‐enhanced nephelometric immunoassay was more preserved in the whole ß‐casein than in its isolated fragments. The protein concentration producing 50% inhibition of the ß‐casein‐coated microparticle agglutination with anti‐native ß‐casein antiserum increased during ß‐casein denaturation. A microparticle‐enhanced nephelometric immunoassay, quantifying changes of this inhibiting protein concentration, permitted detection of alteration of the immunoreactivity of ß‐casein during its plasmin proteolysis and heat denaturation, providing an adequate test for the integrity of the whole molecule.
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