Use of endoproteinase Lys-C from Lysobacter enzymogenes in protein sequence analysis

Anal Biochem. 1983 Oct 15;134(2):347-54. doi: 10.1016/0003-2697(83)90308-1.

Abstract

Endoproteinase Lys-C from Lysobacter enzymogenes, which is commercially available, proved to be useful in the determination of primary structures of proteins. The enzyme preferentially cleaves at the carboxyl side of lysine residues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 4-Hydroxybenzoate-3-Monooxygenase
  • Amino Acid Sequence
  • Bacteria / enzymology*
  • Chemical Phenomena
  • Chemistry
  • Endopeptidases / metabolism*
  • Metalloendopeptidases*
  • Peptide Fragments
  • Ribonuclease, Pancreatic

Substances

  • Peptide Fragments
  • 4-Hydroxybenzoate-3-Monooxygenase
  • Ribonuclease, Pancreatic
  • Endopeptidases
  • Metalloendopeptidases
  • peptidyl-Lys metalloendopeptidase