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Acid optimum kininogenases in canine myocardium and aorta.
Cardiovasc Res
April 1992
Department of Physiology and Pharmacology, University of Strathclyde, Glasgow, United Kingdom.
Objective: Canine coronary artery was recently reported to contain a cathepsin like acid optimum enzyme and a kallikrein like alkaline optimum enzyme which cleaved from a crude kininogen preparation a vasodilator uterus contracting substance. The aim of this study was to seek the presence of similar acid optimum enzymes in canine ventricular myocardium and in a large systemic artery, the aorta.
Methods: Aqueous canine tissue extracts were tested for the ability at different pHs to release uterus contracting substance (using rat isolated oestrous uterus) from a kininogen preparation.
Enzymes in normally perfused and ischaemic dog hearts which release a substance with kinin like activity.
Cardiovasc Res
February 1989
Department of Physiology and Pharmacology, University of Strathclyde, Glasgow, Scotland.
The presence of amidases cleaving the tripeptide VAL.LEU.ARG.
View Article and Find Full Text PDF[3-(1,4-Cyclohexadienyl)-L-alanine,8-lysine]vasopressin, otherwise known as [3-(2,5-dihydrophenylalanine),8-lysine]vasopressin or [DiHPhe3]lysine-vasopressin, has been synthesized in an attempt to utilize 2,5-dihydrophenylalanine (DiHPhe) to evaluate the contribution of aromaticity in position 3 to biological activity. The analogue has the same primary structure as lysine-vasopressin, except that two additional hydrogen atoms are present on the ring moiety of the phenylalanine residue in position 3. The key intermediate was the protected nonapeptide N-carbobenzoxy-S-benzyl-L-cysteinyl-L-tyrosyldihydrophenyl-L-alanyl-L-glutaminyl-L-asparaginyl-S-benzyl-L-cysteinyl-L-prolyl-N epsilon-tosyl-L-lysylglycinamide that was synthesized stepwise by the solid-phase technique.
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