SUCCINYL TRIALANINE p-NITOROANILIDE-HYDROLYTIC ENZYME FROM INSOLUBLE FRACTION OF GUINEA PIG KIDNEY

概要

論文の詳細を見る
Succinyl trialanine p-nitroanilide (STANA)-hydrolytic enzyme was partially purified from insoluble fraction of guinea pig kidney, and its physicochemical and enzymatic properties were investigated. Extraction of the enzyme from the insoluble fraction was achieved with 2% Triton X-100 without much loss of the activity. This enzyme required calcium ion for its full activity, and the additionof EGTA or EDTA led to the reversible or irreversible inactivation, respectively. The apparent molecular weight estimated by gel filtration on Sepharose 4B column after treatment with 2% Triton X-100 was approximately 120,000. The enzyme was stable in pH 4.5 to 8.5, and the optimum pH was 8.0. This enzyme showed high substrate specificity: Amoung several substrates tested, only Suc-(Ala)_3-pNA, an artificial elastase substrate, was very susceptible to this enzyme. Ac-(Ala)_3-pNA was hydrolyzed poorly, and Suc-(Ala)_2-pNA, Suc-Ala-pNA, Bz-Arg-pNA, Bz-Tyr-pNA and elastin (natural elastase substrate) were not hydrolyzed at all. These results were compared with the previous data on liver STANA-hydrolytic enzymes and the correlation between them was discussed.
名古屋市立大学の論文
1984-03-26