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PMID: 2995131 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin.

FEBS letters ·Vol. 190 ·No. 1 ·1985-10-07 ·Pages 81-3

Harris HE

Abstract

G-Actin-ATP bound to plasma gelsolin to form a 2:1 complex. The complex contained approximately equivalent amounts of nucleotide and actin. More than 84% of this nucleotide was ATP. Half of the bound nucleotide was displaced by cold chase and the remainder did not exchange, implying that the two actins in the complex are not equivalent.

MeSH Terms

Actins/blood Adenosine Diphosphate/blood Adenosine Triphosphate/blood Animals Calcium-Binding Proteins/blood Chromatography, Gel Gelsolin Microfilament Proteins/blood Protein Binding Rabbits Swine

Chemicals

Actins Calcium-Binding Proteins Gelsolin Microfilament Proteins Adenosine Diphosphate Adenosine Triphosphate

Authors & Affiliations

1 authors, click to expand affiliations / ORCID

Harris H E

Article Info

Journal

FEBS letters

Abbr.

FEBS Lett

ISSN

0014-5793

DOI

10.1016/0014-5793(85)80432-4

Published

1985-10-07

Pages

81-3

Language

English

Region

England

NLM ID

0155157

Subset

External Links

PubMed source DOI: 10.1016/0014-5793(85)80432-4 View journal details

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Lack of nucleotide cleavage on the binding of G-actin-ATP to plasma gelsolin.

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