JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Ikemoto, N.
Right arrow Articles by Nelson, R. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ikemoto, N.
Right arrow Articles by Nelson, R. W.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 259, Issue 19, 11790-11797, 10, 1984

Oligomeric regulation of the later reaction steps of the sarcoplasmic reticulum calcium ATPase

N Ikemoto and RW Nelson

The phosphorylated intermediate of the sarcoplasmic reticulum Ca2+ ATPase (EP) was formed from [gamma-32P] ATP, and its decomposition was monitored by chasing with either ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) or an excess amount of [gamma- 31P]ATP. Chasing in the initial phase of E32P formation leads to monophasic and rapid decomposition, whereas chasing after the maximal level of E32P has been reached leads to biphasic decomposition. If a portion of EPtotal is formed from [gamma-31P]ATP (E31P) and the rest from [gamma-32P]ATP (E32P), decomposition of the later portion (E32P) is roughly monophasic and the rate of decomposition is about the same as that of the slow phase of the biphasic decomposition. Initiation of the EP reaction by concurrent addition of [gamma-32P]ATP and EGTA, conditions that permit the selective monitoring of the EP reaction via one of the subunits of the putative dimer (Ikemoto, N., Garcia, A. M., Kurobe, Y., and Scott, T. L. (1981) J. Biol. Chem. 256, 8593-8601) leads to monophasic decomposition at a rate comparable with the fast phase of biphasic decomposition. The kinetics of biphasic EP decomposition is reversibly affected by the nonionic detergent ethylene glycol monoether and the cleavable cross-linker dithiobissuccinimidyl propionate, both of which presumably affect subunit-subunit interactions. The results suggest that the biphasic EP decomposition is due to sequential liberation of Pi from different subunits (EI and EII) forming an oligomer as shown in the following model.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
C. V. Filomatori and A. F. Rega
On the Mechanism of Activation of the Plasma Membrane Ca2+-ATPase by ATP and Acidic Phospholipids
J. Biol. Chem., June 13, 2003; 278(25): 22265 - 22271.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
J. Nakamura and G. Tajima
Independence of Two Conformations of Sarcoplasmic Reticulum Ca2+-ATPase Molecules in Hydrolyzing Acetyl Phosphate. A TWO-PAIR MODEL OF THE ATPase STRUCTURAL UNIT
J. Biol. Chem., August 1, 1997; 272(31): 19290 - 19294.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1984 by the American Society for Biochemistry and Molecular Biology.