The regulation of ATPase-ATPase interactions in sarcoplasmic reticulum membrane. I. The effects of Ca2+, ATP, and inorganic phosphate.

L. Dux, A. Martonosi

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Abstract

Two-dimensional crystalline arrays of Ca2+-ATPase molecules develop after treatment of sarcoplasmic reticulum vesicles with Na3VO4 in calcium-free medium (Dux, L., and Martonosi, A. (1983) J. Biol. Chem. 258, 2599-2603). The formation of Ca2+-ATPase crystals is inhibited by Ca2+ (2 microM), or ATP (5 mM), but not by ADP, 5'-adenylylimidodiphosphate, or adenylylmethylenediphosphonate. ATPase crystals did not form at 37 degrees C and exposure of preformed crystals to 37 degrees C for 1 h caused the disappearance of crystal lattice. Inorganic orthophosphate (1 mM at pH 6.0) promoted the formation of a distinct crystal form of Ca2+-ATPase, which was different from that produced by Na3VO4. These observations indicate that Ca2+, ATP, inorganic phosphate, pH, and temperature influence the interactions between ATPase molecules in the sarcoplasmic reticulum membrane.

Original languageEnglish
Pages (from-to)11896-11902
Number of pages7
JournalJournal of Biological Chemistry
Volume258
Issue number19
Publication statusPublished - Oct 10 1983

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Calcium-Transporting ATPases
Sarcoplasmic Reticulum
Adenosine Triphosphatases
Adenosine Triphosphate
Phosphates
Membranes
Crystals
Adenylyl Imidodiphosphate
Adenosine Diphosphate
Molecules
Crystal lattices
Calcium
Temperature
Crystalline materials

ASJC Scopus subject areas

  • Biochemistry

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The regulation of ATPase-ATPase interactions in sarcoplasmic reticulum membrane. I. The effects of Ca2+, ATP, and inorganic phosphate. / Dux, L.; Martonosi, A.

In: Journal of Biological Chemistry, Vol. 258, No. 19, 10.10.1983, p. 11896-11902.

Research output: Contribution to journalArticle

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