Identification of a high molecular weight alkaline protease in rat heart.
We have identified in soluble extracts of rat heart, a 500 000 dalton sulfhydryl-dependent protease which degrades globin and casein to acid-soluble peptides at an alkaline pH optimum. This enzyme was purified more than 1700-fold with respect to the postmicrosomal supernatant. On the basis of various catalytic and biochemical properties the enzyme appears similar to a recently described cytoplasmic protease in rat liver. Protease activity in vitro was stimulated up to 3-fold by physiologic concentrations of ATP and to a lesser extent by some other phosphate-containing compounds. Unlike some alkaline proteases reported in heart tissue, this high molecular weight protease was identified in extracts from isolated cardiac myocytes and in extracts from hearts of rats treated with the mast cell degranulating agent Compound 48/80. Thus, the identification of the protease in heart does not appear to be accounted for by mast cell contamination.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008297:Male; D008970:Molecular Weight; D009206:Myocardium / Q000032:analysis / Q000166:cytology / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000032:analysis* / Q000378:metabolism; D051381:Rats; D013439:Sulfhydryl Reagents / Q000378:metabolism
D013439:Sulfhydryl Reagents; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases