ISSN:
1420-9071
Keywords:
Pig kidney cortex
;
des-Arg-bradykinin
;
angiotensin I-converting enzyme
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Medicine
Notes:
Summary Fast and very slow hydrolyses of des-Arg9-bradykinin and angiotensin II by angiotensin I-converting enzyme were detected by high performance liquid chromatography. The Michaelis constants of the enzyme, Km values, for des-Arg9-bradykinin and bradykinin were found to be 0.24 mM and 4.4 μM, and the maximum velocities, Vmax values (μmol·min−1·mg protein−1) for these compounds to be 3.24 and 0.34, respectively. The enzyme also hydrolyzed Z-Gly-Pro-Gly-Gly-Pro-Ala to a tripeptide that was identified as dansyl-Gly-Pro-Ala by TLC on polyamide. These observations show that the enzyme hydrolyzes the peptides at the bond before the prolyl residue in the penultimate position.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF02004493
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