Action of brain cathepsin B,cathepsin D,and high-molecular-weight aspartic proteinase on angiotensins I and II |
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Authors: | Anahit Azaryan Nina Barkhudaryan Armen Galoyan Abel Lajtha |
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Institution: | (1) Institute of Biochemistry, Sevak str 5/1, 375044 Yervan, USSR;(2) Center for Neurochemistry Ward's Island, 10035 New York, New York |
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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.
Special Issue dedicated to Dr. Eugene Kreps. |
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