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Neurochemical Research

, Volume 10, Issue 11, pp 1525–1532 | Cite as

Action of brain cathepsin B, cathepsin D, and high-molecular-weight aspartic proteinase on angiotensins I and II

  • Anahit Azaryan
  • Nina Barkhudaryan
  • Armen Galoyan
  • Abel Lajtha
Original Articles

Abstract

The action of three previously isolated electrophoretically homogeneous brain proteinases—cathepsin B (EC 3.4.22.1), cathepsin D (EC 3.4.23.5), and high-molecular-weight aspartic proteinase (Mr=90K; EC 3.4.23.−)—on human angiotensins I and II has been investigated. The products of enzymatic hydrolysis have been identified by thin-layer chromatography on Silufol plates using authentic standards and by N-terminal amino acid residue analysis using a dansyl chloride method. Cathepsin D and high-molecular-weight aspartic proteinase did not split angiotensin I or angiotensin II. Cathepsin B hydrolyzed angiotensin I via a dipeptidyl carboxypeptidase mechanism removing His-Leu to form angiotensin II, and it degraded angiotensin II as an endopeptidase at the Val3-Tyr4 bond. Cathepsin B did not split off His-Leu from Z-Phe-His-Leu. Brain cathepsin B may have a role in the generation and degradation of angiotensin II in physiological conditions.

Keywords

Angiotensin Enzymatic Hydrolysis Endopeptidase Homogeneous Brain Authentic Standard 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Publishing Corporation 1985

Authors and Affiliations

  • Anahit Azaryan
    • 1
  • Nina Barkhudaryan
    • 1
  • Armen Galoyan
    • 1
  • Abel Lajtha
    • 2
  1. 1.Institute of BiochemistryYervanUSSR
  2. 2.Center for Neurochemistry Ward's IslandNew York

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