黒緑豆モヤシカタラーゼ:酵素学的・タンパク質的性質

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The enzymatic and protein-chemical properties were investigated in catalase purified from black matpe (Phaseolus mungo L. var. radiatus Bak) sprouts. The catalase had a broad optimum pH of 7 to 9 in 0.05M phosphate buffer and Tris-HCl buffer. The enzyme was very labile below pH 6.0 but relatively stable at pH 9.0. It was slowly inactivated by dilution and was rapidly inactivated by 8M urea. About 20% of the enzyme activity was lost by freezing and thawing. Low molecular weight nitrogen compounds including NH2OH•HCl, NaN3, KCN, NaNO2, CS(NH2)2 and 3-amino-1, 2, 4-triazole were potent inhibitors of the enzyme. The sedimentation coefficient (s20, W) of the enzyme was 12.1 s. The molecular weight was determined as 187, 000 by the sedimentation equilibrium method using a partial specific volume of 0.72. The protein was characterized by a high content of serine, glutamic acid and glycine, as well as by a low content of cystine and methionine.
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