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INFLUENCE OF MUTATION IN ε SUBUNIT OF Escherichia coli H^+-ATPase COMPLEX (F_1F_0) ON BIOCHEMICAL PROPERTIES OF THE ENZYME
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作者 吴季辉 林治焕 《Chinese Science Bulletin》 SCIE EI CAS 1991年第5期404-408,共5页
The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<... The membrane-bound H<sup>+</sup>-ATPase of E. coil consisted of two parts: F<sub>1</sub> and F<sub>0</sub>. Purified ε subunit of F<sub>1</sub> strongly inhibited F<sub>1</sub> but showed no inhibitory effect in reconstituted F<sub>1</sub>F<sub>0</sub>. In 1987, G. B. Cox et al. isolated a mutant of ε subunit, and two partial revertants, Their experiments showed that F<sub>1</sub>F<sub>0</sub> complex was still formed in the mutant. The hydrolytic activity and transmembrane proton transfer ability were all impaired in the 展开更多
关键词 ESCHERICHIA coli F1F0 εsubunit mutation.
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