Protease, Staph aureus (Endoproteinase Glu-C) Product Information

Source: Staphylococcus aureus V8

I.U.B.: 3.4.21.19

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.

Unit Definition: One Unit causes a change of 0.001 A₂₈₀ nm per minute at 37°C, pH 7.8 using casein as the substrate.

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