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.-Reference-Cited by-同舟云学术

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.

Published:1981-09 Issue:17 Volume:256 Page:9084-9089
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Esch F S,Böhlen P,Otsuka A S,Yoshida M,Allison W S

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference12 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. The Mitochondrial ATPase. Evidence for a Single Essential Tyrosine Residue

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