FRAGMENTATION OF BOVINE CHROMOGRANIN-A BY PLASMA KALLIKREIN

被引：23

作者：

LEDUC, R

HENDY, GN

SEIDAH, NG

CHRETIEN, M

LAZURE, C

机构：

[1] CLIN RES INST MONTREAL, JA DESEVE LAB MOLEC NEUROENDOCRINOL, MONTREAL H2W 1R7, QUEBEC, CANADA

[2] ROYAL VICTORIA HOSP, MONTREAL H3A 1A1, QUEBEC, CANADA

[3] MCGILL UNIV, MONTREAL H3A 1A1, QUEBEC, CANADA

来源：

LIFE SCIENCES | 1990年 / 46卷 / 20期

基金：

英国医学研究理事会;

关键词：

D O I：

10.1016/0024-3205(90)90458-4

中图分类号：

R-3 [医学研究方法]; R3 [基础医学];

学科分类号：

1001 ;

摘要：

Chromogranin A has been reported to be processed in vivo by an as yet undefined proteinase(s) suggesting that it is a precursor of biologically active peptides such as pancreastatin. In this study, plasma kallikrein was used as a model proteinase to identify the cleavage sites exposed in bovine parathyroid chromogranin A. Purified bovine parathyroid chromogranin A was digested with human plasma kallikrein. The proteolytic fragments produced were isolated by HPLC and chemically characterized by amino acid composition and sequence analysis. The combined results indicate that the enzyme has preference for specific single Arg residues, cutting C-terminal to this amino acid, although certain pairs of basic sites were also cleaved. The characterized fragments were released in a selective manner from the whole molecule with rapid production of the fragments covering positions 1-247 and 352-358. © 1990.

引用

页码：1427 / 1433

页数：7

共 27 条

[1] PRIMARY STRUCTURE OF BOVINE PITUITARY SECRETORY PROTEIN-I (CHROMOGRANIN-A) DEDUCED FROM THE CDNA SEQUENCE [J].