Factors influencing [3H]ryanodine binding to the skeletal muscle Ca2+ release channel

Analytical Biochemistry
D H Needleman, S L Hamilton

Abstract

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 a diffusion limited process, and often the binding reaches a peak value which is followed by a slow decline. This phenomenon makes it extremely difficult to determine kinetic constants for [3H]ryanodine binding. The inclusion of bovine serum albumin (BSA) or the detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate (Chaps) in the incubation buffer prevents the decrease in [3H]ryanodine binding observed in association studies. BSA or Chaps slows this decline in binding partially by preventing a conversion to a more rapidly dissociating component. Pretreatment of the membranes with Chaps does not prevent the decrease in [3H]ryanodine binding, suggesting that Chaps is not exerting its effect by extracting a lipid or peripheral membrane protein. The decrease in affinity observed in the absence of BSA and Chaps appears to require the occupation of the high-affinity ryanodine binding site. Incubation for extended times in th...Continue Reading

References

Sep 8, 1992·Molecular and Cellular Biochemistry·G Meissner, A el-Hashem
Jan 1, 1989·Annual Review of Biophysics and Biophysical Chemistry·S Fleischer, M Inui
Oct 1, 1984·Physiological Reviews·A N Martonosi
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Jan 1, 1994·Critical Reviews in Biochemistry and Molecular Biology·Y Ogawa
May 1, 1994·Analytical Biochemistry·G Zardeneta, P M Horowitz

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Citations

Feb 23, 2007·American Journal of Physiology. Cell Physiology·Julio A CopelloLothar A Blatter
Jan 14, 1999·The American Journal of Physiology·J Z ZhangS L Hamilton

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