Literature DB >> 6967064

Heterogeneity of amino acid incorporation rate in adult skeletal muscle actin.

K Kohama.   

Abstract

An actin preparation extracted at 25 degree C for 2 h from the residue which had previously been subjected to the routine extraction procedure, i.e. at 4 degree C for 15 min, showed markedly increased rates of amino acid incorporation, i.e. 48% higher than routinely extracted actin. The nature of the actin having higher amino acid incorporation rates was discussed in relation to 10S-actinin.

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Year:  1980        PMID: 6967064     DOI: 10.1093/oxfordjournals.jbchem.a132832

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Myosin light-chain kinase of smooth muscle stimulates myosin ATPase activity without phosphorylating myosin light chain.

Authors:  L H Ye; H Kishi; A Nakamura; T Okagaki; T Tanaka; K Oiwa; K Kohama
Journal:  Proc Natl Acad Sci U S A       Date:  1999-06-08       Impact factor: 11.205

2.  Myosin light chain kinase from skeletal muscle regulates an ATP-dependent interaction between actin and myosin by binding to actin.

Authors:  K Fujita; L H Ye; M Sato; T Okagaki; Y Nagamachi; K Kohama
Journal:  Mol Cell Biochem       Date:  1999-01       Impact factor: 3.396

  2 in total

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