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A Ca 2+ ‐sensitive actin regulatory protein from smooth muscle
Author(s) -
Kanno Kimiyoshi,
Sasaki Yasuharu,
Hidaka Hiroyoshi
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80607-4
Subject(s) - egta , actin , size exclusion chromatography , affinity chromatography , sephadex , chemistry , polymerization , biophysics , cytoplasm , biochemistry , calcium , biology , enzyme , organic chemistry , polymer
Using a procedure involving DNase I affinity chromatography and Sephadex G‐200 gel filtration, we partially purified a Ca 2+ ‐sensitive actin regulatory 90‐kDa protein from bovine aorta. The 90‐kDa protein existed in the form of a complex with actin on a DNase I column even in the presence of 5 mM EGTA, indicating that the 90‐kDa protein binds tightly to actin in a Ca 2+ ‐insensitive manner. The isolation procedure described above indicates that the 90‐kDa protein is present in smooth muscles including aorta, uterus and bladder, but not in skeletal and heart muscles. When added to G‐actin before polymerization, the 90‐kDa protein increases the initial rate of actin polymerization and lowers the final viscosity at Ca 2+ concentrations greater than 10 −7 M. This decrease in viscosity is due to the generation of filaments which cannot be readily sedimented.