Am J Physiol Cell Physiol Track the topics, authors and articles important to you
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 258: C185-C188, 1990;
0363-6143/90 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Zhao, D. Y.
Right arrow Articles by Dhalla, N. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Zhao, D. Y.
Right arrow Articles by Dhalla, N. S.

AJP - Cell Physiology, Vol 258, Issue 1 C185-C188, Copyright © 1990 by American Physiological Society

ARTICLES

[35S]ATP gamma S binding sites in the purified heart sarcolemma membrane

D. Y. Zhao and N. S. Dhalla
Division of Cardiovascular Sciences, St. Boniface General Hospital Research Centre, Winnipeg, Manitoba, Canada.

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.


This article has been cited by other articles:


Home page
 Physiol. Rev.Home page
G. Vassort
Adenosine 5'-Triphosphate: a P2-Purinergic Agonist in the Myocardium
Physiol Rev, April 1, 2001; 81(2): 767 - 806.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online