Results 151 to 160 of about 975 (184)
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Purification of a myotoxin from the toadfish Thalassophryne maculosa (Günter) venom
Toxicon, 2005Venom was milked by gently pressing the base of the opercular and dorsal fin spines. Three fractions were obtained by molecular exclusion high pressure liquid chromatography (HPLC) (Protein Pak 125SW, Millipore Corporation) column, but only the last one with 22.7 min retention time (rt) was biological active (TmPP-22.7).
J I, Sosa-Rosales +4 more
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A common cytolytic region in myotoxins, hemolysins, cardiotoxins and antibacterial peptides*
International Journal of Peptide and Protein Research, 1989Several proteins and polypeptides of reptilian, amphibian, insect, and microbial origin share a common cytolytic property. However, these cytolysins fulfill different objectives. They provide offensive armament in the case of toxins, but defensive systems in the case of antibacterial peptides.
R M, Kini, H J, Evans
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Interaction of myotoxin a with the Ca2+-ATPase of skeletal muscle sarcoplasmic reticulum
Archives of Biochemistry and Biophysics, 1986Myotoxin a is a muscle-damaging toxin isolated from the venom of Crotalus viridis viridis. Its interaction with the Ca2+-ATPase of sarcoplasmic reticulum (SR) vesicles purified from rabbit skeletal muscle was investigated. Myotoxin a inhibited Ca2+ loading and stimulated Ca2+-dependent ATPase without affecting unidirectional Ca2+ efflux. Its action was
P, Volpe, E, Damiani, A, Maurer, A T, Tu
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Antiserum to myotoxin from prairie rattlesnake (Crotalus viridis viridis) venom
Toxicon, 1979Abstract C. L. Ownby , W. M. Woods and G. V. Odell . Antiserum to myotoxin from prairie rattlesnake ( Crotalus viridis viridis ) venom. Toxicon 17, 373–380. 1979.—A myotoxic component was isolated from rattlesnake ( Crotalus viridis viridis ) venom and an antibody to it was produced in rabbits. Gel-filtration and cation exchange chromatography
C L, Ownby, W M, Woods, G V, Odell
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LOCAL ANESTHETICS ARE POTENT MYOTOXINS
Southern Medical Journal, 1999Radoslav Kosanin, Verne Lanier
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A Novel Myotoxin from the Venom of Trimeresurus mucrosquamatus.
Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica SinicaA novel myotoxin, designated TMPB, was purified from the venom of Trimeresurus mucrosquamatus by Sephadex G-100 superfine gel chromatography and fast protein liquid chromatography (FPLC). The N-terminal sequence of 24 amino acid residues was determined by protein sequencer. The sequence similarities between TMPB and other two phospholipase A(2) (PLA2s)
Tian-Rui, Xu +5 more
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Expression of recombinant ACL myotoxin in E. coli
Toxicon, 1996H.S.Selistre de Araujo, C.L. Ownby
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