Literature DB >> 945265

Beta-actinin-like protein from plasmodium.

K Maruyama, R Kamiya, S Kimura, S Hatano.   

Abstract

A beta-actinin-like protein was isolated from plasmodia of the slime mold. The chain weight was the same as that of actin (43,000), but the amino acid composition was significantly different. The action of plasmodium beta-actinin on actin was the same as that of beta-actinin from rabbit skeletal muscle: inhibition of the recombination of F-actin fragments; formation of Mg polymer; inhibition of interfilamental interaction of F-actin and retardation of depolymerization of F-actin. The only difference observed was its sensitivity to trypsin: plasmodium actinin was less quickly digested by trypsin than rabbit beta-actinin.

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Year:  1976        PMID: 945265     DOI: 10.1093/oxfordjournals.jbchem.a131122

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


  3 in total

1.  Biochemistry of actomyosin-dependent cell motility (a review).

Authors:  E D Korn
Journal:  Proc Natl Acad Sci U S A       Date:  1978-02       Impact factor: 11.205

2.  A compilation of amino acid analyses of proteins : XVII. Residues per thousand residues-4.

Authors:  D M Kirschenbaumt
Journal:  Appl Biochem Biotechnol       Date:  1982-09       Impact factor: 2.926

3.  Analysis of the mechanism of fast axonal transport by intracellular injection of potentially inhibitory macromolecules: evidence for a possible role of actin filaments.

Authors:  D J Goldberg; D A Harris; B W Lubit; J H Schwartz
Journal:  Proc Natl Acad Sci U S A       Date:  1980-12       Impact factor: 11.205

  3 in total

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