コイ筋小胞体の精製およびその性状〔英文〕

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Fragmented sarcoplasmic reticulum (FSR) was separated from carp ordinary muscle and purified into light (LSR), intermediate, and heavy sarcoplasmic reticulum (HSR) fractions by a sucrose gradient method. Electron microscopy disclosed that most vesicles in FSR fraction were round-shaped, with a few elliptical and asymmetric vesicles. LSR fraction was rich in elliptical and tubule vesicles, while HSR fraction showed many round vesicles with feet structures.Polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate revealed that these fractions had a 97, 000 (97k) Da component as the major. Two ?? 70kDa and one each of 35kDa and 10kDa components exhibited a Ca2+-binding ability in 45Ca autoradiography.Ca2+-ATPase and Ca2+ uptake activities of carp FSR were highly dependent on temperature, both being reduced with decreasing reaction temperature.
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