Preparation and some chemical characteristics of milk-clotting protease from Bacillus mesentericus 76

Int J Pept Protein Res. 1981 Jan;17(1):89-92. doi: 10.1111/j.1399-3011.1981.tb01971.x.

Abstract

Pure milk-clotting protease (MCP-76) is isolated by isotachophoresis at pH 5.0. The native molecule has only one protein chain. It is a metaloenzyme containing zinc. The pure MCP-76 has a molecular weight of 33 000 (+/- 1500) and by diphenyl-indenonyl-isothiocyanate method showed arginine as N-terminal amino acid.

MeSH terms

  • Animals
  • Aspartic Acid Endopeptidases*
  • Aspergillus / isolation & purification
  • Bacillus / enzymology*
  • Cattle
  • Endopeptidases / isolation & purification*
  • Milk*
  • Molecular Weight

Substances

  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • rennin-like enzyme (Aspergillus ochraceus)