A myosin-like protein from smooth muscle.
A protein was purified from chicken gizzard smooth muscle. It bound ATP and actin. Actin activated the Mg2(+)-ATPase activity of this protein. The Ca2(+)-ATPase activity was lower than K(+)-EDTA ATPase activity. Thus, it appears that this protein is akin to myosin I rather than to conventional myosin. However, ATPase activities of the protein were much lower than those of myosin I. A protein cofactor, such as protein kinase, which would enhance these activities remains to be purified from the smooth muscle.
Kohama
K
K
Department of Pharmacology, Gunma University School of Medicine, Japan.
Lin
Y
Y
Takano-Ohmuro
H
H
Ishikawa
R
R
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D009130:Muscle, Smooth / Q000737:chemistry* / Q000378:metabolism; D009218:Myosins / Q000302:isolation & purification* / Q000378:metabolism
D000199:Actins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins