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Similar Ca 2+ dependences of [ 3 H]ryanodine binding to α‐ and β‐ryanodine receptors purified from bullfrog skeletal muscle in an isotonic medium
Author(s) -
Murayama Takashi,
Ogawa Yasuo
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00053-1
Subject(s) - ryanodine receptor , bullfrog , skeletal muscle , gene isoform , chemistry , calcium , biophysics , receptor , biochemistry , biology , endocrinology , organic chemistry , gene
To understand the functions of the two ryanodine receptor isoforms (α‐ and β‐RyRs) in nonmammalian skeletal muscles, we determined [ 3 H]ryanodine binding to these isoforms purified from bullfrog skeletal muscle. In 0.17 M‐NaCl medium, both isoforms demonstrated similar Ca 2+ dependent ryanodine binding activities, while the Ca 2+ sensitivity for activation of β‐RyR was increased in 1 M‐NaCl medium. This enhancement in Ca 2+ sensitivity depended on the kind of salts used. These results imply that α‐ and β‐RyRs may have similar properties as Ca 2+ ‐induced Ca 2+ release channels in bullfrog skeletal muscle.