Literature DB >> 3782072

The 45K molecular weight actin-modulating protein from sea urchin eggs forms a complex with actin in the presence of calcium ions.

M Ohnuma, I Mabuchi.   

Abstract

The 45K protein from sea urchin eggs forms a complex with actin in the presence of Ca2+. The fraction was not readily dissociated on depletion of Ca2+ by gel filtration, but was dissociated on dialysis against an EGTA-containing solution. The free 45K protein and the 45K protein-actin complex affect F-actin in different manners in the presence of Ca2+. The former severs F-actin in the presence of Ca2+ but not in its absence, while the latter caps the barbed end of F-actin in a Ca2+-independent manner thereby lowering the viscosity of F-actin slowly.

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Year:  1986        PMID: 3782072     DOI: 10.1093/oxfordjournals.jbchem.a121776

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


  4 in total

1.  The 50 kDa protein-actin complex from unfertilized sea-urchin (Strongylocentrotus purpuratus) eggs. Interaction with actin.

Authors:  R M Golsteyn; D M Waisman
Journal:  Biochem J       Date:  1989-02-01       Impact factor: 3.857

2.  The purification of a 50 kDa protein-actin complex from unfertilized sea-urchin (Strongylocentrotus purpuratus) eggs.

Authors:  R M Golsteyn; D M Waisman
Journal:  Biochem J       Date:  1989-02-01       Impact factor: 3.857

Review 3.  Cellular and molecular aspects of oocyte maturation and fertilization: a perspective from the actin cytoskeleton.

Authors:  Luigia Santella; Nunzia Limatola; Jong Tai Chun
Journal:  Zoological Lett       Date:  2020-04-15       Impact factor: 2.836

4.  The F-actin capping proteins of Physarum polycephalum: cap42(a) is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap42(b) is Physarum actin.

Authors:  C Ampe; J Vandekerckhove
Journal:  EMBO J       Date:  1987-12-20       Impact factor: 11.598

  4 in total

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