Abstract
To understand the functions of the two ryanodine receptor isoforms (alpha- and beta-RyRs) in nonmammalian skeletal muscles, we determined [3H]ryanodine binding to these isoforms purified from bullfrog skeletal muscle. In 0.17 M-NaCl medium both isoforms demonstrated similar Ca2+ dependent ryanodine binding activities, while the Ca2+ sensitivity for activation of beta-RyR was increased in 1 M-NaCl medium. This enhancement in Ca2+ sensitivity depended on the kinds of salts used. These results imply that alpha- and beta-RyRs may have similar properties as Ca2+-induced Ca2+ release channels in bullfrog skeletal muscle.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphate / analogs & derivatives
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Adenosine Triphosphate / pharmacology
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Animals
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Caffeine / pharmacology
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Calcium / pharmacology*
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Calcium Channels / drug effects
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Calcium Channels / isolation & purification
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Calcium Channels / metabolism*
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Cholic Acids / pharmacology
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Muscle Proteins / drug effects
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Muscle Proteins / isolation & purification
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Muscle Proteins / metabolism*
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Muscle, Skeletal / chemistry*
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Phospholipids / pharmacology
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Rana catesbeiana
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Ryanodine / metabolism*
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Ryanodine Receptor Calcium Release Channel
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Sodium Chloride
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Tritium
Substances
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Calcium Channels
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Cholic Acids
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Muscle Proteins
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Phospholipids
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Ryanodine Receptor Calcium Release Channel
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Tritium
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Ryanodine
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5'-adenylyl (beta,gamma-methylene)diphosphonate
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Caffeine
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Sodium Chloride
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Adenosine Triphosphate
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alpha,beta-methyleneadenosine 5'-triphosphate
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3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate
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Calcium