Purification and characterisation of swine serum proteinase which hydrolyses epidermal inhibitory pentapeptide

Biochim Biophys Acta. 1996 Jun 4;1290(2):184-90. doi: 10.1016/0304-4165(96)00018-9.

Abstract

In this paper we describe the purification to molecular homogeneity of the enzyme that cleaves the synthetic epidermal mitosis-inhibiting pentapeptide (pyroGlu-Glu-Asp-Ser-Gly; EPP) from swine serum. Biochemical characterisation of the enzyme shows a glycoprotein with apparent molecular mass of 200 kDa. The Km and Kcat values for EPP hydrolysis are 0.624 mM and 694 s-1, respectively. Use of proteinase inhibitors shows the enzyme's metalloendopeptidase character. Moreover, captopril and lisinopril prevent the cleavage of EPP. The N-terminal amino-acid sequence of the purified protein corresponds to the N-terminal amino-acid sequence of swine kidney angiotensin-converting enzyme, a dipeptidyl carboxypeptidase (EC 3.4.15.1).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensin-Converting Enzyme Inhibitors / pharmacology
  • Animals
  • Captopril / pharmacology
  • Carboxypeptidases / blood*
  • Carboxypeptidases / chemistry
  • Enzyme Inhibitors / pharmacology
  • Glycoproteins / chemistry
  • Growth Inhibitors / blood
  • Growth Inhibitors / metabolism*
  • Kinetics
  • Lisinopril / pharmacology
  • Molecular Sequence Data
  • Oligopeptides / metabolism*
  • Peptidyl-Dipeptidase A / metabolism*
  • Pyrrolidonecarboxylic Acid / analogs & derivatives
  • Substrate Specificity
  • Swine

Substances

  • Angiotensin-Converting Enzyme Inhibitors
  • Enzyme Inhibitors
  • Glycoproteins
  • Growth Inhibitors
  • Oligopeptides
  • epidermal pentapeptide
  • Captopril
  • Lisinopril
  • Carboxypeptidases
  • Peptidyl-Dipeptidase A
  • Pyrrolidonecarboxylic Acid