Physical and chemical properties of extracellular staphylococcal lipase.
Highly purified staphylococcal lipase was subjected to physico-chemical analysis. Effect of ionic strength and of protein structure modifying agents supports views suggesting the subunit structure of this enzyme. Chelating and reducing agents, thiol group inhibitors, and bile acid salts do not influence the enzyme activity. Digestion of purified staphylococcal lipase with proteolytic enzymes indicates that lipase is sensitive to trypsin, alpha-chymotrypsin and pronase.
D019791:Guanidine; D006146:Guanidines / Q000494:pharmacology; D008049:Lipase / Q000378:metabolism*; D009821:Oils / Q000378:metabolism; D009994:Osmolar Concentration; D010447:Peptide Hydrolases / Q000494:pharmacology; D011136:Polysorbates / Q000378:metabolism; D012965:Sodium Chloride / Q000494:pharmacology; D013210:Staphylococcus / Q000201:enzymology*; D013379:Substrate Specificity; D014508:Urea / Q000494:pharmacology
D006146:Guanidines; D009821:Oils; D011136:Polysorbates; D012965:Sodium Chloride; D014508:Urea; D008049:Lipase; D010447:Peptide Hydrolases; D019791:Guanidine