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

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

doi:10.1016/S0006-291X(86)80104-8

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 journal › Article › peer-review

12 Scopus citations

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 language	English (US)
Pages (from-to)	235-243
Number of pages	9
Journal	Biochemical and Biophysical Research Communications
Volume	139
Issue number	1
DOIs	https://doi.org/10.1016/S0006-291X(86)80104-8
State	Published - Aug 29 1986
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

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title = "Solubilization and separation of Ca2+-ATPase from the Ca2+-ryanodine receptor complex",

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.",

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AU - Casida, John E.

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N2 - 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.

AB - 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.

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