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A new scorpion polypeptide enhances the binding of radiolabeled-ryanodine on ryanodine receptor in sarcoplasmic reticulum of rabbit skeletal muscle 被引量:1

A new scorpion polypeptide enhances the binding of radiolabeled-ryanodine on ryanodine receptor in sarcoplasmic reticulum of rabbit skeletal muscle
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摘要 RYANODINE is a toxic alkaloid from the plant Ryania speciosa Vahl. It selectively binds to the Ca<sup>2+</sup> release channel on skeletal and cardiac heavy sarcoplasmic reticulum (HSR) and has
出处 《Chinese Science Bulletin》 SCIE EI CAS 1997年第2期147-151,共5页
关键词 SCORPION Buthus martensi Karsch RYANODINE receptor TOXIC polypeptide. scorpion Buthus martensi Karsch ryanodine receptor toxic polypeptide
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  • 1吉永华,H.Hattori,徐科,S.Terakawa.Molecular Characteristics of Four New Depressant Insect Neurotoxins Purified From Venom of Buthus martensi Karsch by HPLC[J].Science China Chemistry,1994,37(8):955-963. 被引量:3
  • 2Pessah,I. N.,Francini,A. O.,Scales,D. J.,Waterhouse,A. L.,Casidia,J. E.Calcium-ryanodine receptor complex. Journal of Biological Chemistry . 1986
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  • 4Valdivia H,Fuentes O,Elhayek R. et al.Activation of the ryanodine receptor Ca2+ release channel of sarcoplasmic reticulum by a novel scorpion venom. Journal of Biological Chemistry . 1991
  • 5Valdivia,H H et al.Direct binding of verapamil to the ryanodine receptor channel of sarcoplasmic reticulum, Biophys. J . 1990
  • 6Laemmli U K.Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature . 1970
  • 7Loret E P,Martin-Eauclaire M F,Mansuelle P et al.An anti-insect toxin purified from the scorpion Androctonus australis Hector also acts on the α- and β-sites of the mammalian sodium channel: sequence and circular dichroism study. Biochemistry . 1991

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