The specificity of carboxyl group modification during the inactivation of the Escherichia coli F1-ATPase with dicyclohexyl[14C]carbodiimide.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference27 articles.
1. Reactivity of mitochondrial F1-ATPase to dicyclohexylcarbodiimide. Inactivation and binding studies
2. Inactivation of Escherichia coli BF1-ATPase by dicyclohexylcarbodiimide. Chemical modification of the .beta. subunit
3. The interaction of N,N'-dicyclohexylcarbodiimide with chloroplast coupling factor 1.
4. Identification of an essential glutamic acid residue in the beta subunit of the adenosine triphosphatase from the thermophilic bacterium PS3.
5. Inactivation of the bovine mitochondrial F1-ATPase with dicyclohexyl[14C]carbodiimide leads to the modification of a specific glutamic acid residue in the beta subunit.
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