Title : Ca2+ binding sites of the ryanodine receptor/Ca2+ release channel of sarcoplasmic reticulum. Low affinity binding site(s) as probed by terbium fluorescence.

Pub. Date : 1994 Oct 7

PMID : 7929166






4 Functional Relationships(s)
Download
Sentence
Compound Name
Protein Name
Organism
1 Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. tb3+ ryanodine receptor 1 Homo sapiens
2 Fluorescence spectroscopy has been used to study the interaction of Tb3+ (as a Ca2+ analog) with the purified ryanodine receptor (RyR)/Ca2+ release channel of skeletal muscle sarcoplasmic reticulum. tb3+ ryanodine receptor 1 Homo sapiens
3 About 20% of the bound Tb3+ was not displaced by EGTA or Ca2+; suggesting its "occlusion" in the RyR. tb3+ ryanodine receptor 1 Homo sapiens
4 The results suggest that RyR/Ca2+ release channel undergoes conformational changes due to Tb3+ binding to the low-affinity Ca2+ binding site, and this binding results in the closing of the Ca2+ release channel. tb3+ ryanodine receptor 1 Homo sapiens