INTERACTIONS BETWEEN STAPHYLOCOCCAL PROTEIN-A AND IMMUNOGLOBULIN DOMAINS

被引：62

作者：

LANCET, D ^{[1
]}

ISENMAN, D ^{[1
]}

SJODAHL, J ^{[1
]}

SJOQUIST, J ^{[1
]}

PECHT, I ^{[1
]}

机构：

[1] UNIV UPPSALA,CTR BIOMED,DEPT MED & PHYSIOL CHEM,S-75105 UPPSALA,SWEDEN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1978年 / 85卷 / 02期

关键词：

D O I：

10.1016/0006-291X(78)91206-8

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The affinity and stoichiometry of interaction between staphylococcal protein A and different domains of immunoglobulins have been studied. Light scattering and tryptophan fluorescence quenching titrations along with direct binding assays were performed. The lack of binding to protein A of pFc′ fragment (corresponding to CH3 domain of IgG) or of Facb derivative of rabbit IgG (which is devoid of the CH3) suggests that the locus of protein A binding is at the interface between the CH2 and CH3 domains. This assignment is also supported by results of the tryptophan fluorescence quenching and C1 binding experiments. © 1978.

引用

页码：608 / 614

页数：7

共 30 条

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[19] LANCET D, UNPUBLISHED
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