The Dicyclohexylcarbodiimide-Binding Protein of Rat Liver Mitochondria as a Product of the Mitochondrial Protein Synthesis
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12423.x/fullpdf
Reference37 articles.
1. The Properties of Dicyclohexylcarbodiimide as an Inhibitor of Oxidative Phosphorylation*
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3. Isolation of a chloroplast N,N'-dicyclohexylcarbodiimide-binding proteolipid, active in proton translocation.
4. Purification of the carbodiimide-reactive protein component of the ATP energy-transducing system of Escherichia coli.
5. Purification of the DCCD-reactive protein of the energy-transducing adenosine triphosphatase complex fromEscherichia coli
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1. A Study of the Dicyclohexylcarbodiimide-Binding Component of the Mitochondrial ATPase Complex from Beef Heart;European Journal of Biochemistry;2005-03-03
2. Electrophoretic behavior of the H+-ATPase proteolipid from bovine heart mitochondria;Journal of Bioenergetics and Biomembranes;1986-12
3. Studies on polypeptide composition, hydrolytic activity and proton conduction of mitochondrial F0F1 H+ ATPase in regenerating rat liver;European Journal of Biochemistry;1986-03
4. Biosynthetic pathway of mitochondrial ATPase subunit 9 in Neurospora crassa.;Journal of Cell Biology;1983-01-01
5. Proton-transporting urinary epithelia. Reactivity with N,N′-dicyclohexylcarbodiimide;Biochimica et Biophysica Acta (BBA) - Bioenergetics;1982-05
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