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Inhibition of calcium-dependent actin gelation by actin-binding protein from platelets.

作者信息

Sasaki A, Hiyoshi M, Hashimoto K, Im T, Tatsumi N, Okuda K

机构信息

Department of Clinical and Laboratory Medicine, Osaka City University Medical School.

出版信息

Biochem Int. 1990 Aug;21(5):823-30.

PMID:2256944
Abstract

Various proteins related to cell contraction have been extracted from human platelets. Of these, a protein (48K) with the molecular weight of 48,000 and one with the molecular weight of 47,000 (P47) often migrate together with actin on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. We studied the biochemical characteristics of the 48K protein, purified by actin affinity and DEAE-Sepharose chromatography. The 48K protein did not react with anti-actin antibody or peroxidase-labelled actin. The protein inhibited the calcium-dependent gelation of actin. The 48K protein seemed to be a regulatory protein involving cell contraction not identified before.

摘要

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