Solubilization and separation of Ca2+-ATPase from the Ca2+-ryanodine receptor complex

Isaac N Pessah, Kenneth W. Anderson, John E. Casida

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Heavy sarcoplasmic reticulum (SR) preparations of rabbit skeletal muscle, which are enriched in Ca2+-release vesicles from the terminal cisternae (TC) and [3H]ryanodine receptor density, exhibit 60% of the Ca2+-ATPase activity, 58% of the EP level, and 30% of the steady state Ca2+-loading compared to membrane vesicles from the longitudinal SR. The Ca2+-ATPase of TC SR is solubilized and separated from the Ca2+-ryanodine receptor complex in the insoluble fraction on treatment with the detergent C12E9. However, a 50% decrease in receptor density is observed upon removal of the Ca2+-ATPase, suggesting a significant contribution of this protein to maintaining optimal receptor complex density.

Original languageEnglish (US)
Pages (from-to)235-243
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume139
Issue number1
DOIs
StatePublished - Aug 29 1986
Externally publishedYes

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Ryanodine Receptor Calcium Release Channel
Calcium-Transporting ATPases
Sarcoplasmic Reticulum
Detergents
Muscle
Skeletal Muscle
Rabbits
Membranes
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Solubilization and separation of Ca2+-ATPase from the Ca2+-ryanodine receptor complex. / Pessah, Isaac N; Anderson, Kenneth W.; Casida, John E.

In: Biochemical and Biophysical Research Communications, Vol. 139, No. 1, 29.08.1986, p. 235-243.

Research output: Contribution to journalArticle

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