HUMAN SERUM AMYLOID-P COMPONENT BINDS TO A SPECIFIC PEPTIDE IN THE PRESENCE OF CALCIUM

被引：3

作者：

HAMAZAKI, H

机构：

[1] Kitasato Univ., Sch. Med., Department Biol., Sagamihara

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 205卷 / 02期

关键词：

D O I：

10.1006/bbrc.1994.2789

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：

Human serum amyloid P component (SAP) binds to a carboxyl-terminal peptide of residues 160-204 of SAP itself in the presence of calcium. A set of sequentially overlapping decapeptides covering the entire length of residues 160-204 of SAP was synthesized on polyethylene pins to be used for binding assay, and six overlapping peptides in residues 190-204(Tyr-Glu-Ile-Arg-Gly-Tyr-Val-Ile-Ile-Lys-Pro-Leu-Val-Trp-Val) were found to have equally high affinity for SAP. The validity of using peptides on polyethylene pins was shown by the binding assay using 11-residue soluble peptide corresponding to residues 194-204. Replacement of the Lys or the lie residues with Glu abolished the binding activity. (C) 1994 Academic Press, Inc.

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页码：1172 / 1178

页数：7

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