Re-Investigation of the Protein Structure of Coenzyme B12-Dependent Diol Dehydrase
Re-Investigation of the Protein Structure of Coenzyme B12-Dependent Diol Dehydrase
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辅酶 B12 依赖性二醇脱水酶蛋白质结构的重新研究
DOI:
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发表时间:
1987
期刊:
影响因子:
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通讯作者:
K. Soda
中科院分区:
文献类型:
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作者:
K. Tanizawa;N. Nakajima;T. Toraya;Hidehiko Tanaka;K. Soda
We have purified diol dehydrase, an adenosylcobalamin-dependent enzyme, from Klebsiella pneumoniae by two different procedures to re-investigate its protein structure; one including its extraction with detergent from the membrane fraction, and the other consisting of only chromatographic separations of the soluble fraction. The enzyme preparations obtained by these two methods were different in the subunit structure, but both are identical in molecular weight, and in enzymological and immunochemical properties. In addition, the enzyme preparation obtained from the membrane fraction dissociated reversibly into two dissimilar protein components (F and S) in the absence of substrate, as did the preparation from the soluble fraction. Although the subunit multiplicity of component S might be partly due to proteolytic cleavage during the enzyme purification as revealed by limited digestion with trypsin, component F is not a product of proteolytic cleavage of component S, but a primordial and essential constituent of the enzyme.