Protease, S. aureus V8 (Endoproteinase Glu-C)

Blue Ice

27

Supplied as a lyophilized powder.

Endoproteinase-Glu-C Protease from S. aureus V8 specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acid. In the presence of ammonium buffers, 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. It is 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).

Activity:
≥500 units per mg dry weight

Absorbance (A280) at 1mg/ml:
As reported

Unit Definition:
One Unit causes a change of 0.001 absorbance unit (at 280nm) per minute at 37°C, pH 7.8 using casein as the substrate.

Extinction Coefficient:
4.26

Optimum pH:
4.0 and 7.8 with hemoglobin substrate

Inhibitors:
Diisopropyl fluorophosphate (DFP) and monovalent anions such as F-, Cl-, Br-, CH3COO-, and NO3-

Quality Control:
SDS-PAGE

Storage and Stability:
Stable for 6 months after receipt at 4ºC. Autolysis occurs at temperatures greater than 40ºC. The enzyme is fully active in 2mg/ml SDS.