HETEROGENEITY OF SMOOTH-MUSCLE MYOSIN LIGHT CHAIN KINASE IS REVEALED BY ANION-EXCHANGE HIGH-PERFORMANCE LIQUID-CHROMATOGRAPHY

被引：6

作者：

FASOLO, M ^{[1
]}

CAVALLINI, P ^{[1
]}

DALLALIBERA, L ^{[1
]}

机构：

[1] INST GEN PATHOL,NATL RES COUNCIL,MUSCLE BIOL & PHYSIOPATHOL UNIT,VIA TRIESTE 75,I-35100 PADUA,ITALY

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 175卷 / 01期

关键词：

D O I：

10.1016/S0006-291X(05)81231-8

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：

When smooth muscle myosin light chain kinase, purified by standard procedures from chicken gizzard smooth muscle, was applied to an anion-exchange high-performance liquid chromatographic column, three well resolved peaks were obtained. Each peak contained a single protein whose electrophoretic mobility corresponded to that of MLCK. However each enzyme was characterized by a different specific activity. Peptide mapping experiments were unable to demonstrate different proteolytic patterns for the three proteins. Treatment of myosin light chain kinase with alkaline phosphatase, prior to ion chromatography, resulted in a change of elution profile. These experiments suggest that myosin light chain kinase could exist in three forms characterized by a different degree of phosphorylation. © 1991 Academic Press, Inc.

引用

页码：277 / 284

页数：8

共 9 条

[1]

CAVALINI P, 1988, SARCOMERIC NONSARCOM, P677

[2]

DALLALIBERA L, 1990, BIOCHEM BIOPH RES CO, V167, P1249

[3]

GARONE ML, IN PRESS SMOOTH MUSC

[4] THE PROTEIN-KINASE FAMILY - CONSERVED FEATURES AND DEDUCED PHYLOGENY OF THE CATALYTIC DOMAINS [J].