A novel alkaline proteinase associated with the actomyosin complex from pig uterine myometrium.
A novel proteolytic activity has been demonstrated an partially characterized in the actomyosin complex isolated from smooth uterine muscle. This proteolytic activity showed an alkaline pH optimum, was inhibited by SH-group-blocking reagents but not by metal-chelating agents and copurified with the actomyosin complex. An important characteristic of this alkaline proteolytic activity was that it seems to hydrolyze the actomyosin by limited proteolysis with a concomitant loss of the myosin adenosinetriphosphatase activity.
D000205:Actomyosin / Q000378:metabolism*; D000818:Animals; D005260:Female; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008970:Molecular Weight; D009215:Myometrium / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D013552:Swine; D014599:Uterus / Q000201:enzymology*
D000205:Actomyosin; D010447:Peptide Hydrolases