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ÖÐÎÄÃû³Æ £º µ°°×øS


ÆäËûÖÐÎÄÃû³Æ £º V8µ°°×øS


Ó¢ÎÄÃû³Æ £º Protease S Aureus


ÆäËûÓ¢ÎÄÃû³Æ £º Endoproteinase Glu-C from Staphylococcus aureus V8£»V8 Protease


C A S £º 66676-43-5


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À´ Ô´ £º Staph aureus V8


Activity £º ¡Ý500units/mg


»îÁ¦¶¨Òå £º One Unit causes a change of 0.001 A280 nm per minute at 37¡æ, pH 7.8 using casein as the substrate


²úÆ·ÃèÊö £º Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids. In the presence of ammonium, the enzyme specificity is limited to glutamic sites. It has a molecular weight of 27,000 daltons and optimum pH's of 4.0 and 7.8 with hemoglobin as the substrate. Protease S. aureus V8 is inhibited by diisopropylfluorophosphate and monovalent anions such as F-, Cl-, CH3COO- and NO3. Enzyme activity is determined by the casein digestion assay described by Drapeau (Methods Enzymol., 45, 469, 1976).


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