Inhibition of calcium-dependent actin gelation by actin-binding protein from platelets.
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.
Sasaki
A
A
Department of Clinical and Laboratory Medicine, Osaka City University Medical School.
Hiyoshi
M
M
Hashimoto
K
K
Im
T
T
Tatsumi
N
N
Okuda
K
K
D000199:Actins / Q000737:chemistry* / Q000276:immunology; D001792:Blood Platelets / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism*; D002846:Chromatography, Affinity; D005782:Gels; D006801:Humans; D008840:Microfilament Proteins / Q000378:metabolism / Q000494:pharmacology*; D008970:Molecular Weight
D000199:Actins; D005782:Gels; D008840:Microfilament Proteins; D002118:Calcium