Evidence for myosin-binding phosphatase in heart myofibrils

被引:16
作者
Nishio, H [1 ]
Ichikawa, K [1 ]
Hartshorne, DJ [1 ]
机构
[1] UNIV ARIZONA,MUSCLE BIOL GRP,TUCSON,AZ 85721
基金
美国国家卫生研究院;
关键词
D O I
10.1006/bbrc.1997.7005
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
Protein phosphatase was partially purified from myofibrils of bovine heart by sequential column chromatographies. The purified protein phosphatase was immunologically identified as a delta isoform of PP1 (PP1 delta). The myosin-binding subunit (MBS) of myosin-binding phosphatase (MBP) in smooth muscle was co-purified with PP1 delta at each step of the sequential column chromatographies. The immunoprecipitation experiment using the polyclonal antibody to MBS showed that PP1 delta associates with MBS in the purified phosphatase. In addition, the myosin-binding assay showed that the purified phosphatase has the characteristics of binding to cardiac myosin. These data strongly suggest that MBP, the holoenzyme composed of PP1 delta and MBS, is expressed in heart myofibrils. (C) 1997 Academic Press.
引用
收藏
页码:570 / 575
页数:6
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