Phosphoenzyme conformational states and nucleotide-binding site hydrophobicity following thiol modification of the Ca2+-ATPase of sarcoplasmic reticulum from skeletal muscle.-Reference-Cited by-同舟云学术

Phosphoenzyme conformational states and nucleotide-binding site hydrophobicity following thiol modification of the Ca2+-ATPase of sarcoplasmic reticulum from skeletal muscle.

Published:1987-05 Issue:15 Volume:262 Page:7041-7046
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Davidson G A,Berman M C

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference40 articles.

1. MECHANISM OF FREE ENERGY COUPLING IN ACTIVE TRANSPORT

2. Substrate regulation of the sarcoplasmic reticulum ATPase. Transient kinetic studies.

3. Induction by nucleotide triphosphate hydrolysis of a form of sarcoplasmic reticulum ATPase capable of medium phosphate-oxygen exchange in presence of calcium.

4. Adenosine 5'-triphosphate modulation of catalytic intermediates of calcium-adenosine triphosphatase of sarcoplasmic reticulum subsequent to enzyme phosphorylation

5. Transient kinetic analysis of turnover-dependent fluorescence of 2‘,3‘-O-(2,4,6-trinitrophenyl)-ATP bound to Ca2+-ATPase of sarcoplasmic reticulum.

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