Protease, Staph aureus (Endoproteinase Glu-C)
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).
Stability/Storage: Autolysis occurs at temperatures greater than 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C.
Carboxypeptidase B (COBC/COBPMS)
Carboxypeptidase Y (COY)Chymotrypsin (CDAG/CDI/CDS/CDTLCK)
Clostripain, Endo-Arg-C (CP)
Neutral Protease (Dispase, NPRO)
Proteinase K (PROK)
Trypsin, SequENZ (TRSEQII/TRSEQZ)