Description
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 kDa 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.
Abbr
V8 Protease, Native (Staph aureus V8)
Product Overview
Protease S. aureus V8 (Endoproteinase-Glu-C) specifically cleaves peptide bonds on the COOH-terminal side of either aspartic or glutamic acids.
Enzyme Commission Number
EC 3.4.21.19
Activity
> 500 units per mg dry weight
Molecular Weight
27 kDa (Drapeau 1978).
Purity
Chromatographically purified
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.
Optimum pH
4.0 and 7.8 with hemoglobin substrate. (Drapeau et al. 1972).
Stability
Autolysis occurs at temperatures > 40°C. The enzyme is fully active in USP 0.2% SDS. Stable for 12 months at 2-8°C.
Inhibitors
Diisopropyl fluorophosphate (DFP) and monovalent anions such as F-, Cl-, Br-, CH3COO-, and NO3-(Houmard 1976).
Synonyms
EC 3.4.21.19; Staph aureus V8 Protease; Protease, Staph aureus (Endoproteinase Glu-C); Glutamyl endopeptidase; V8 proteinase, endoproteinase Glu-C; staphylococcal serine proteinase
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