Identification of the dicyclohexylcarbodiimide-binding protein in the oligomycin-sensitive adenosine triphosphatase from bovine heart mitochondria

Biochemistry ◽  
1972 ◽  
Vol 11 (7) ◽  
pp. 1144-1150 ◽  
Author(s):  
Feico S. Stekhoven ◽  
Richard F. Waitkus ◽  
Herman Th. B. Van Moerkerk
1975 ◽  
Vol 148 (3) ◽  
pp. 533-537 ◽  
Author(s):  
R B Beechey ◽  
S A Hubbard ◽  
P E Linnett ◽  
A D Mitchell ◽  
E A Munn

An almost pure form of the bovine heart mitochondrial adenosine triphosphatase (ATPase) is released from the membrane by shaking submitochondrial particles with chloroform. Analyses on polyacrylamide gels and by electron microscopy, and also sensitivity to inhibitors, show that the chloroform-released enzyme is similar to other ATPase preparations from bovine heart mitochondria.


1965 ◽  
Vol 240 (1) ◽  
pp. 29-33
Author(s):  
Leslie T. Webster ◽  
Lance D. Gerowin ◽  
Louis Rakita

1989 ◽  
Vol 264 (26) ◽  
pp. 15548-15551
Author(s):  
S Joshi ◽  
M J Pringle

1987 ◽  
Vol 17 (1) ◽  
pp. 147-152
Author(s):  
G. Lippe ◽  
A. Perardi ◽  
M.C. Sorgato ◽  
F. Dabbeni-Sala

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