Chemical crosslinking and enzyme kinetics provide no evidence for a regulatory role for the 53 kDa glycoprotein of sarcoplasmic reticulum in calcium transport-Reference-Cited by-同舟云学术

Chemical crosslinking and enzyme kinetics provide no evidence for a regulatory role for the 53 kDa glycoprotein of sarcoplasmic reticulum in calcium transport

Published:1991-04 Issue:1 Volume:1064 Page:139-147
ISSN:0005-2736
Container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Biomembranes

Author:

Burgess A.J.,Matthews I.,Grimes E.A.,Mata A.M.,Munkonge F.M.,Lee A.G.,East J.M.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference39 articles.

1. Purification and Properties of an Adenosine Triphosphatase from Sarcoplasmic Reticulum

2. Energy Interconversion by the Ca2+-Dependent ATPase of the Sarcoplasmic Reticulum

3. Amino-acid sequence of a Ca2+ + Mg2+ -dependent ATPase from rabbit muscle sarcoplasmic reticulum, deduced from its complementary DNA sequence

4. A kinetic model for the Ca2+ + Mg2+-activated ATPase of sarcoplasmic reticulum

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

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4. Anionic phospholipids decrease the rate of slippage on the Ca2+-ATPase of sarcoplasmic reticulum;BIOCHEM J;1999

5. Complex formation between calsequestrin and the ryanodine receptor in fast- and slow-twitch rabbit skeletal muscle;FEBS Letters;1998-06-16