Tonin-like activity present in the human submandibular gland

Agents Actions Suppl. 1992:38 ( Pt 1):392-400. doi: 10.1007/978-3-0348-7321-5_49.

Abstract

An enzyme which is able to liberate angiotensin II from angiotensin I, angiotensinogen(1-14) fragment and angiotensinogen was purified from human submandibular gland. Its molecular weight is 110,000; is inhibited by PMSF but not by EDTA or enalaprilat. The pH optima for angiotensin II liberation were 4.0 for angiotensin I, 7.0 for angiotensinogen(1-14) fragment and 8.0 for angiotensinogen. The total amount of angiotensin II generating activity in the human submandibular gland is 5,000-times smaller than that in the rat gland.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensin I / chemistry
  • Angiotensin II / chemistry
  • Angiotensinogen / chemistry
  • Humans
  • Molecular Sequence Data
  • Molecular Weight
  • Peptidyl-Dipeptidase A / chemistry
  • Peptidyl-Dipeptidase A / isolation & purification*
  • Peptidyl-Dipeptidase A / metabolism
  • Submandibular Gland / enzymology*
  • Substrate Specificity

Substances

  • Angiotensinogen
  • Angiotensin II
  • Angiotensin I
  • Peptidyl-Dipeptidase A