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• W2079381878 abstract "Abstract Urinary kallikrein (urokallikrein), as defined by its capacity to generate kinin from heat-inactivated plasma or from purified human kininogen, was isolated from fresh concentrated male human urine and shown to be an antigenically unique urinary p -tosyl-L-arginine methyl ester HCl (TAMe) esterase. The isolation procedure achieved a 400- to 576-fold purification of the kinin-generating activity/mg of protein and yielded a product with albumin as the only significant contaminant at the isoelectric focusing step. The purified urokallikrein, defined by its kinin-generating activity, exhibited an isoelectric point with a range from pH 3.9 to 4.2 with charge heterogeneity, an apparent molecular weight of 25,000–40,000 on Sephadex gel filtration, and an anodal mobility on alkaline disc gels. Urokallikrein eluted from disc gels and identified by kinin-generating activity elicited monospecific antiserum in the rabbit. That purified urokallikrein is a TAMe esterase was evident from the concordance of kinin-generating activity, antigenic reactivity with a donkey antipancreas serum shown to recognize urokallikrein and esterolytic capacity as assessed after isoelectric focusing. There was suppression of the esterolytic activity of purified urokallikrein by increasing doses of TAMe or benzoyl-L-arginine methyl ester HCl (BAMe), and analysis of these data with Dixon plots indicated substrate inhibition." @default.
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• W2079381878 date "1977-10-01" @default.
• W2079381878 modified "2023-09-27" @default.
• W2079381878 title "Kinin-generating and esterolytic activity of purified human urinary kallikrein (urokallikrein)" @default.
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• W2079381878 doi "https://doi.org/10.1016/0006-2952(77)90163-0" @default.
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