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.
Size
1 mg
Concentration
1 mg/mL
Applications
Protease S. aureus has shown that one unit causes a change of 0.001 A280 nm per minute at 37° C at pH 7.8 using casein as a substrate. Specific conditions for reactivity should be optimized by end user.