Reduction of disulfide bonds in sarcoplasmic reticulum Ca(2+)-ATPase by dithiothreitol causes inhibition of phosphoenzyme isomerization in catalytic cycle. This reduction requires binding of both purine nucleotide and Ca2+ to enzyme-Reference-Cited by-同舟云学术

Reduction of disulfide bonds in sarcoplasmic reticulum Ca(2+)-ATPase by dithiothreitol causes inhibition of phosphoenzyme isomerization in catalytic cycle. This reduction requires binding of both purine nucleotide and Ca2+ to enzyme

Published:1994-04 Issue:15 Volume:269 Page:11060-11064
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Daiho T.,Kanazawa T.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference22 articles.

1. ADENOSINE TRIPHOSPHATE-LINKED CONCENTRATION OF CALCIUM IONS IN A PARTICULATE FRACTION OF RABBIT MUSCLE

2. Two Ca2+ ATPase genes: Homologies and mechanistic implications of deduced amino acid sequences

3. Mechanism of Calcium Transport

4. The reactivity of the thiol groups of the adenosine triphosphatase of sarcoplasmic reticulum and their location on tryptic fragments of the molecule

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