PHOTOAFFINITY-LABELING OF THE PRIMARY FIBRIN POLYMERIZATION SITE - LOCALIZATION OF THE LABEL TO GAMMA-CHAIN TYR-363

被引：64

作者：

YAMAZUMI, K ^{[1
]}

DOOLITTLE, RF ^{[1
]}

机构：

[1] KAGOSHIMA UNIV,SCH MED,DEPT SURG 1,KAGOSHIMA 890,JAPAN

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 1992年 / 89卷 / 07期

关键词：

FIBRINOGEN; FRAGMENT-D;

D O I：

10.1073/pnas.89.7.2893

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Fragment D prepared from human fibrinogen was labeled specifically by photoactivation of the peptide [C-14]Gly-Pro-Arg-N-(4-azido-2-nitrophenyl)Lys amide. The preparation was freed of excess labeling reagents and then reduced and alkylated. The component alpha, beta, and gamma-chains were purified by chromatography on carboxymethylcellulose and the radioactivity was found to be restricted to the gamma-chain. Isolated gamma-chains were digested with various endopeptidases, both alone and in tandem, and the products were fractionated by gradient HPLC. The amino acid compositions of all labeled peptides led to the conclusion that the modification occurs exclusively on gamma-chain Tyr-363.

引用

页码：2893 / 2896

页数：4

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