A contribution to the skeletal structure of ryanodine
✍ Scribed by D.R. Babin; J.A. Findlay; T.P. Forrest; F. Fried; M. Gőtz; Z. Valenta; K. Wiesner
- Publisher
- Elsevier Science
- Year
- 1960
- Tongue
- French
- Weight
- 431 KB
- Volume
- 1
- Category
- Article
- ISSN
- 0040-4039
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Rabbit skeletal muscle homogenates were fractionated by differential centrifugation over the range 2,000-35,000 x G, and the calcium pumping activity of each fraction was assayed, together with the sensitivity of this activity to ryanodine. The greatest ryanodine sensitivity was found in material se
Optimal [3H]ryanodine binding to skeletal muscle sarcoplasmic reticulum membranes is dependent on a number of factors such as Ca2+ concentration, ionic strength, and the presence of modulators of the Ca2+ release channel. The rate of association of [3H]-ryanodine with its binding site is slower than