Literature DB >> 6444873

Calcium-sensitivity of pig-carotid-actomyosin ATPase in relation to phosphorylation of the regulatory light chain.

U Mrwa, M Troschka, C Gross, L Katzinski.   

Abstract

Ca2+-dependent phosphorylation of the 20000-Mr regulatory light chain was found to be a necessary condition for the Ca2+-sensitivity of the Mg2+-dependent ATPase activity and superprecipitation of pig carotid actomyosin. Actin-myosin interaction independent of phosphorylation and Ca2+ (ATPase activity and superprecipitation) were demonstrated in aged actomyosin preparations and in preparations from which the regulatory light chains were removed by papain digestion.

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Year:  1980        PMID: 6444873     DOI: 10.1111/j.1432-1033.1980.tb04328.x

Source DB:  PubMed          Journal:  Eur J Biochem        ISSN: 0014-2956


  4 in total

1.  Simple model of smooth muscle myosin phosphorylation and dephosphorylation as rate-limiting mechanism.

Authors:  J W Peterson
Journal:  Biophys J       Date:  1982-02       Impact factor: 4.033

2.  A Ca2+-sensitive myosin light chain kinase, regulating pig carotid smooth muscle actomyosin ATPase.

Authors:  L Katzinski; U Mrwa
Journal:  Experientia       Date:  1980-03-15

3.  Contraction in intact pig aortic strips is not always associated with phosphorylation of myosin light chains.

Authors:  K J Murray; P J England
Journal:  Biochem J       Date:  1980-12-15       Impact factor: 3.857

4.  Effect of calcium-antagonist and calmodulin-antagonist drugs on calmodulin-dependent contractions of chemically skinned vascular smooth muscle from rabbit renal arteries.

Authors:  V A Kreye; J C Rüegg; F Hofmann
Journal:  Naunyn Schmiedebergs Arch Pharmacol       Date:  1983-06       Impact factor: 3.000

  4 in total

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