heart cell membrane
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1994 ◽  
Vol 26 (2) ◽  
pp. 211-218 ◽  
Author(s):  
Hiroshi Okamoto ◽  
Hideaki Kawaguchi ◽  
Hitoshi Sano ◽  
Ken Kageyama ◽  
Toshiyuki Kudo ◽  
...  

1990 ◽  
Vol 258 (1) ◽  
pp. C185-C188 ◽  
Author(s):  
D. Y. Zhao ◽  
N. S. Dhalla

Purified heart sarcolemma membranes were found to bind a slowly hydrolyzable analogue of ATP [35S-labeled adenosine 5'-(gamma-thio)triphosphate [( 35S]ATP gamma S)] in a specific manner and exhibited two apparent affinity sites. The high-affinity site had a dissociation constant (KD) of 4.7-8.3 nM [maximum binding (Bmax) = 9.5-18.4 pmol/mg protein], whereas the low-affinity site had a KD of 655-1,257 nM (Bmax = 812-2,955 pmol/mg protein). Like ATP, other nucleotides such as GTP, UTP, ITP, and CTP were effective in displacing [35S]ATP gamma S binding. Although crude membrane preparations from different tissues also exhibited both high- and low-affinity sites for [35S]ATP gamma S, KD values for the high affinity sites were severalfold higher than that for the purified heart membranes. It is proposed that the high-affinity binding site for nucleotides may represent the ATP receptor in the heart cell membrane.


Nature ◽  
1979 ◽  
Vol 278 (5703) ◽  
pp. 459-461 ◽  
Author(s):  
ERLAND ERDMANN ◽  
WOLFGANG KRAWIETZ ◽  
GUNTHER PHILIPP ◽  
INGELORE HACKBARTH ◽  
WILHELM SCHMITZ ◽  
...  

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