Effects of trypsin treatment on the structure and function of solubilized coupling factor-latent ATPase from Mycobacterium phlei
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference15 articles.
1. Separation of a Factor Indispensable for Coupled Phosphorylation from the Particulate Fraction of Mycobacterium phlei
2. Energy-transducing membrane-bound coupling factor-ATPase from Mycobacterium phlei. I. Purification, homogeneity, and properties
3. Oxidative phosphorylation in fractionated bacterial systems XLIII. Coupling factors associated with the NAD+-linked electron transport pathway
4. Purification and properties of membrane-bound coupling factor-latent ATPase from mycobacterium phlei
Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. The ϵ subunit as an ATPase inhibitor of the F1-ATPase in Escherichia coli;Archives of Biochemistry and Biophysics;1984-02
2. Use of trypsin to monitor conformational changes of mitochondrial adenosine triphosphatase induced by nucleotides and phosphate;Biochemistry;1983-02-15
3. Polymorphism and conformational dynamics of F1-ATPases from bacterial membranes a model for the regulation of these enzymes on the basis of molecular plasticity;Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes;1982-05
4. Effect of proteolytic digestion on the Ca2+-ATPase activity and subunits of latent and thiol-activated chloroplast coupling factor 1.;Journal of Biological Chemistry;1982-05
5. STRUCTURE AND FUNCTION OF MEMBRANE-BOUND PROTEINS FROM M. phlei;From Cyclotrons to Cytochromes;1982
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