Novel activity of angiotensin-converting enzyme. Hydrolysis of cholecystokinin and gastrin analogues with release of the amidated C-terminal dipeptide
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چکیده
منابع مشابه
wuthering heights and the concept of marality/a sociological study of the novel
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15 صفحه اولthe evaluation of language related engagment and task related engagment with the purpose of investigating the effect of metatalk and task typology
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15 صفحه اولdetection of volatile compounds of medicinal plants with some nano-sorbents using modified or new methodologies and investigation of antioxidant activity of their methanolic extracts
in this work, a novel and fast method for direct analysis of volatile compounds (davc) of medicinal plants has been developed by holding a filament from different parts of a plant in the gc injection port. the extraction and analysis of volatile components of a small amount of plant were carried out in one-step without any sample preparation. after optimization of temperature, extraction time a...
comparison of catalytic activity of heteropoly compounds in the synthesis of bis(indolyl)alkanes.
heteropoly acids (hpa) and their salts have advantages as catalysts which make them both economically and environmentally attractive, strong br?nsted acidity, exhibiting fast reversible multi-electron redox transformations under rather mild conditions, very high solubility in polar solvents, fairly high thermal stability in the solid states, and efficient oxidizing ability, so that they are imp...
15 صفحه اولHydrolysis of bradykinin by angiotensin-converting enzyme.
Two dipeptides, phenylalanylarginine (Phe-Arg) and serylproline (Ser-Pro), are released sequentially from bradykinin by angiotensin-converting enzyme purified from hog lungs; chloride increases the rate of release of both dipeptides. Using an automated ninhydrin-reagent method, we studied the kinetics of bradykinin hydrolysis. The reaction proceeded in the absence of chloride; however, the addi...
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ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1989
ISSN: 0264-6021,1470-8728
DOI: 10.1042/bj2620125