Results 191 to 200 of about 2,964 (225)

Structural, Biological and Biochemical Studies of MyotoxinaAnd Homologous Myotoxins

Journal of Toxicology: Toxin Reviews, 1997
AbstractMyotoxin a and a group of closely related, small, basic toxins cause myonecrotic destruction of muscle tissue upon envenomation. The sarcoplasmic reticulum swells and eventually breaks down to small vesicles. Degeneration of myofibrils and myofilaments ensues and loss of the classic striation pattern is apparent.
A. L. Bieber, D. Nedelkov
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Binding of myotoxin a to cultured muscle cells

Toxicon, 1993
The binding of radiolabeled myotoxin a to various cultured cell lines was evaluated. One rat skeletal muscle-derived cell line, L8, bound substantially more myotoxin a than did all all other cell lines examined. Several biophysical parameters of myotoxin a-L8 binding were determined. Binding was saturable with a moderate binding affinity.
B, Baker, A T, Tu, J L, Middlebrook
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Specific In Vitro Biological Activity of Snake Venom Myotoxins

Journal of Neurochemistry, 1993
Abstract: Some snake venoms contain toxins that are reported to be selective for damaging muscle. This specificity can be used to design experiments intended to eliminate muscle. We studied the small myotoxins and fractions IV and V of Bothrops nummifer venom to evaluate their direct effect on cultured muscle cells, neurons, macrophages, and a ...
J L, Brusés, J, Capaso, E, Katz, G, Pilar   +3 more
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Structure-function relationship of myotoxin a using peptide fragments

Archives of Biochemistry and Biophysics, 1992
Myotoxin a, a small basic polypeptide isolated from the venom of prairie rattlesnake (Crotalus viridis viridis), has been shown to bind to sarcoplasmic reticulum (SR) Ca(2+)-ATPase. The attachment of myotoxin a to Ca(2+)-ATPase is believed to cause uncoupling of the calcium pump.
B, Baker, P, Utaisincharoen, A T, Tu
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Amino acid sequences of myotoxins from Crotalus viridis concolor venom

Toxicon, 1987
Myotoxins I and II were isolated from the venom of Crotalus viridis concolor. Complete sequences were derived for each reduced, alkylated toxin with data obtained by a single run on a gas phase sequencer and from fragments derived by cyanogen bromide cleavage. The results demonstrate that microheterogeneity is present in myotoxin II.
A L, Bieber, R H, McParland, R R, Becker
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Effects of myotoxins on skeletal muscle fibers

Progress in Neurobiology, 1995
This review highlights various aspects of a number of experimental myological alterations, induced by different chemical toxicants, including anticholinesterase, colchicine, vincristine, chloroquine, tetanus toxin, botulinum toxin, reserpine and emetine.
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Origins, genomic structure and copy number variation of snake venom myotoxins

Toxicon, 2022
Crotamine, myotoxin a and homologs are short peptides that often comprise major fractions of rattlesnake venoms and have been extensively studied for their bioactive properties. These toxins are thought to be important for rapidly immobilizing mammalian prey and are implicated in serious, and sometimes fatal, responses to envenomation in humans.
Siddharth S. Gopalan, Blair W. Perry, Drew R. Schield, Cara F. Smith, Stephen P. Mackessy, Todd A. Castoe   +5 more
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Interaction of myotoxin with a artificial membranes: Raman spectroscopic investigations

Biochemistry, 1985
Myotoxin a from the venom of Crotalus viridis viridis (prairie rattlesnake) is a small protein which is responsible for myonecrosis. It is a basic protein with 42 amino acid residues of known sequence. Three disulfide bonds give it a highly compact structure.
W K, Liddle, A T, Tu
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Antiserum to myotoxin from prairie rattlesnake (Crotalus viridis viridis) venom

Toxicon, 1979
Abstract 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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Detection of myotoxin a-like proteins in various snake venoms

Toxicon, 1988
Ninety-five venom samples from eight snake genera (Agkistrodon, Bitis, Bothrops, Calloselasma, Crotalus, Sistrurus, Naja and Vipera) including venoms of Crotalus species of different geographical origin were assayed using immunodiffusion or an ELISA for the presence of the small basic protein, myotoxin alpha, known to cause muscle necrosis.
M A, Bober, J L, Glenn, R C, Straight, C L, Ownby   +3 more
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