The Ca2+-ATPase of the Scallop Sarcoplasmic Reticulum Is of a Cold-adapted Type

D. Sato, T. Takahashi, G. Tajima, C. Sato, Y. Nagata, T. Yamamoto, J. Nakamura

Research output: Contribution to journalArticle

Abstract

At 0 to 20°C, the Ca2+-ATPase activity of the scallop sarcoplasmic reticulum (SR) was observed to be 7-60% of the peak activity at 30°C, while the ATPase activity of the rabbit SR was 0-7% of its peak at 55°C. The relative rabbit ATPase activity (0.7-7.0%) at 7-20°C became higher (6-15 times) and lower (1/4-1/2), respectively, by the solubilization of the rabbit ATPase with a detergent, dodecyloctaethylenglycol monoether, and by the reconstitution of the ATPase with asolectin (soybean lecithin). No activity at 0°C remained irrespective of these treatments. The relative scallop ATPase activity at 0-20°C was, however, scarcely affected by such solubilization and reconstitution. In contrast to the rabbit ATPase, the scallop ATPase seems to be capable of operating independently without the help of the membrane lipid at low temperature.

Original languageEnglish
Pages (from-to)33-39
Number of pages7
JournalJournal of Membrane Biology
Volume196
Issue number1
DOIs
Publication statusPublished - 2003 Nov 1

Keywords

  • ATPase
  • Ca
  • Cold-adaptation
  • Membrane lipid
  • Sarcoplasmic reticulum
  • Scallop

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology

Fingerprint Dive into the research topics of 'The Ca<sup>2+</sup>-ATPase of the Scallop Sarcoplasmic Reticulum Is of a Cold-adapted Type'. Together they form a unique fingerprint.

  • Cite this