Ryanodine receptor purified from crayfish skeletal muscle.
The ryanodine receptor was isolated from the sarcoplasmic reticulum of crayfish skeletal muscle. Ryanodine binding to the native fraction was measured by Scatchard analysis and values of 60 nmol/l and 9 pmol/mg were obtained for KD and Bmax respectively. The identity of purified receptor was confirmed by electron microscopy, electrophoresis and incorporation into planar lipid bilayers. At least two conductance states (100 pS and 50 pS) were observed in 100 mmol/l NaCl both for native and purified receptor.
Formelová
J
J
Institute of Molecular Physiology and Genetics, Slovak Academy of Sciences, Bratislava, Czechoslovakia.
Hurnák
O
O
Novotová
M
M
Zachar
J
J
D000818:Animals; D003400:Astacoidea / Q000378:metabolism*; D002118:Calcium / Q000378:metabolism; D004553:Electric Conductivity; D007700:Kinetics; D008051:Lipid Bilayers; D008854:Microscopy, Electron; D009132:Muscles / Q000378:metabolism*; D011950:Receptors, Cholinergic / Q000302:isolation & purification* / Q000378:metabolism / Q000648:ultrastructure; D012433:Ryanodine / Q000378:metabolism*; D019837:Ryanodine Receptor Calcium Release Channel; D012519:Sarcoplasmic Reticulum / Q000378:metabolism
D008051:Lipid Bilayers; D011950:Receptors, Cholinergic; D019837:Ryanodine Receptor Calcium Release Channel; D012433:Ryanodine; D002118:Calcium