A Kinin-Generating Amidase Activated by Trypsin in Rat Urine

概要

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An enzyme which hydrolyzes dog plasma kininogen and prolyl-phenylalanyl-arginine-4-methylcoumaryl-7-amide (Pro-Phe-Arg-MCA) was separated from rat urinary kallikrein (RUK) by diethyl-aminoethyl-cellulose chromatography during the process of isolation of RUK. When some of the properties of this enzyme was examined, the enzyme was found to be a kinin-generating amidase with properties different from those of RUK, with respect to molecular weight and optimum pH for hydrolysis of Pro-Phe-Arg-MCA. Further, the kinin-generating amidase was activated with trypsin. The molecular weight of the kinin-generating amidase treated with or without trypsin was estimated to be 3.3×10^4 or 3.5×10^4,respectively, by gel filtration on a Sephadex G-100 column, these values being smaller than that of RUK (M.W. 3.8×10^4). These results indicate that rat urine contains a kinin-generating amidase of lower molecular weight than RUK, and that this kinin-generating amidase is activated with a reduction in molecular weight by trypsin treatment.
社団法人日本薬学会の論文
1984-11-25