1999
DOI: 10.1590/s0100-879x1999000100007
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Abstract: A new metalloendopeptidase was purified to apparent homogeneity from a homogenate of normal human liver using successive steps of chromatography on DEAE-cellulose, hydroxyapatite and Sephacryl S-200. The purified enzyme hydrolyzed the Pro 7 -Phe 8 bond of bradykinin and the Ser 25 -Tyr 26 bond of atrial natriuretic peptide. No cleavage was produced in other peptide hormones such as vasopressin, oxytocin or Met-and Leu-enkephalin. This enzyme activity was inhibited by 1 mM divalent cation chelators such as EDTA… Show more

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Cited by 2 publications
(2 citation statements)
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References 17 publications
(16 reference statements)
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“…6,22 In the gastrointestinal tract, CD10 expression is limited to microvilli of the small intestinal and biliary epithelium, where it regulates the concentration of bradykinin, cholecystokinin, and other bioactive substances in the postsecretory modification of bile. 4,5,24 The immunostaining pattern of CD10 in the intestinal villi, gallbladder, and bile ducts is consistently strong with continuous apical expression on the brush border, 14,21,30 whereas in hepatocytes CD10 expression is discontinuous, with patchy apical labeling with a canalicular distribution. 4,6,13,21 A few reports also showed that CD10 expression is mostly preserved in benign lesions such as hepatic bile duct adenoma, 36 pyloric gland adenoma of the gallbladder, 24 and benign intrahepatic bile ducts.…”
mentioning
confidence: 99%
“…A metallopeptidase from human liver which degrades bradykinin and atrial natriuretic peptide was purified to homogeneity by Carvalho et al (32). Another possibility is the interference of the Thimet oligopeptidase (EC 3.4.24.15), which has been reported to be the major liver kininase in the rat (33).…”
Section: Discussionmentioning
confidence: 99%