Krishzyme Endoproteinase-Glu-C or Protease S. aureus V8 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 27kDa 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).
The cleavage specificity is at the C-terminal to Glu (E) residues; also Asp (D) under some buffer conditions.
Application:
– Peptide mapping
– Proteomics
– Mass spectrometry
– Protein structure analysis