Tyrosine-311 of a beta chain is the essential residue specifically modified by 4-chloro-7-nitrobenzofurazan in bovine heart mitochondrial ATPase
- 1 May 1985
- journal article
- research article
- Published by Wiley in European Journal of Biochemistry
- Vol. 148 (3), 551-554
- https://doi.org/10.1111/j.1432-1033.1985.tb08875.x
Abstract
A peptide containing an essential tyrosine residue, modified with the nitrobenzofurazan group, was purified from bovine heart mitochondrial ATPase. The composition of the peptide indicates that this tyrosine is residue 311 in the .beta. chain sequence. The problem of the instability of the tyrosyl-nitrobenzofurazan bond was overcome by working throughout at relatively acidic pH and using pepsin digestin of the enzyme.This publication has 22 references indexed in Scilit:
- Identification of an essential β chain lysine residue from bovine heart mitochondrial ATPase specifically modified with nitrobenzofurazanFEBS Letters, 1985
- Identification of the initially NBD-labeled essential tyrosine residue in bovine heart MF1-ATPaseBiochemical and Biophysical Research Communications, 1983
- Inactivation of Rhodospirillum rubrum coupling factor by 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Modification of a tyrosine protected by phosphateBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1983
- Chemical modification of the >β-subunit isolated from a membrane-bound Fo·F1-ATP synthaseBiochemical and Biophysical Research Communications, 1982
- Reactivity of the .beta. subunit of Escherichia coli adenosine triphosphatase with 4-chloro-7-nitrobenzofurazanBiochemistry, 1979
- Reconstitution of oxidative phosphorylation by chemically modified coupling factor F1: differential inhibition of reactions catalyzed by F1 labeled with 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole or 2,3-butanedioneBiochemistry, 1979
- Affinity chromatography of H+-translocating adenosine triphosphatase isolated by chloroform extraction of Rhodospirillum rubrum chromatophores. Modification of binding affinity by divalent cations and activating anionsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- The Mitochondrial ATPaseEuropean Journal of Biochemistry, 1975
- An unusual and reversible chemical modification of soluble beef heart mitochondrial ATPaseFEBS Letters, 1974