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February 1, 1987Journal of Biological Chemistry617 citationsOpen Access

Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle.

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Population

Junctional terminal cisternae of fast skeletal muscle sarcoplasmic reticulum (SR)

Comparison

Solubilization with CHAPS and purification by… vs Original SR vesicles

Design

Preclinical

Key result

Purified ryanodine receptor from fast skeletal muscle bound 393 +/- 65 pmol of ryanodine/mg of protein and structurally corresponded to the feet structures of junctional terminal cisternae.

Authors

MIMakoto InuiASA SaitoSFSidney Fleischer

Discussion

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Overview

Links ryanodine receptor to Ca2+ release in skeletal muscle feet; leaves open human disease relevance and therapeutic targeting.

Structured PICO

P
Population
Junctional terminal cisternae of fast skeletal muscle sarcoplasmic reticulum (SR)
I
Intervention
Solubilization with CHAPS and purification by sequential column chromatography on heparin-agarose and hydroxylapatite
C
Comparator
Original SR vesicles
O
Outcome
Ryanodine binding properties, molecular weight, and structural characteristics by electron microscopysurrogate

The study demonstrates that the ryanodine receptor and Ca2+ release channel represent a functional unit, with the structural unit being the foot structure of the junctional terminal cisternae.

Cite This Study

Inui et al. (1987) studied this question. Purification of ryanodine receptor was evaluated on Ryanodine binding and structural characteristics. Purified ryanodine receptor from fast skeletal muscle bound 393 +/- 65 pmol of ryanodine/mg of protein and structurally corresponded to the feet structures of junctional terminal cisternae.

synapsesocial.com/papers/6a22491242d97c116a7fc4d7https://doi.org/10.1016/s0021-9258(19)75701-9
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