Results 141 to 150 of about 1,216 (181)

Accessibility of the active site of crotoxin B in the crotoxin complex

Toxicon, 1982
Basic phospholipases A and the crotoxin complex isolated from Crotalus durissus terrificus venom exhibited similar initial reaction rates, time course and degree of hydrolysis of synthetic short chain lecithins in the monomeric state. Although monomeric lecithins seem to promote dissociation of crotoxin up to a certain extent, this cannot explain the ...
G, Canziani, C, Seki, J C, Vidal
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The active components of crotoxin

Biochemical and Biophysical Research Communications, 1972
Summary The main component of Crotalus durissus terrificus venom, crotoxin, represents a natural complex of two types of proteins of isoelectric points at pH 3.7 and 8.6 and molecular weights of about 9000 and 12,000 daltons, respectively. The neurotoxicity of that venom requires the synergistic action of both, while the lecithin requiring ...
J, Horst, R A, Hendon, H, Fraenkel-Conrat   +2 more
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Fractionation and composition of crotoxin

Archives of Biochemistry and Biophysics, 1956
Abstract 1. 1. Crotoxin, upon treatment with fluorodinitrobenzene, yields a water-soluble dinitrophenyl derivative, and a fraction which is insoluble in water and various salt solutions buffered between pH 5 and 10. The latter usually comprises about 65% of the total. 2. 2. The two DNP-proteins differ in their content in most amino acids. The
H, FRAENKEL-CONRAT, B, SINGER
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On the subunit structure of crotoxin: Hydrodynamic and shape properties of crotoxin, phospholipase a and crotapotin

Biochemical and Biophysical Research Communications, 1975
Abstract This paper reports physical-chemical properties of the subunit structure of crotoxin, phospholipase A and crotapotin. The native crotoxin has a sedimentation coefficient of 3S and a radius of gyration of Rg = 16.5 A and a molecular weight of 30,900.
H H, Paradies, H, Breithaupt
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Amino-acid Composition of Crotoxin

Nature, 1951
THE first snake-venom prepared in the pure crystalline form was crotoxin from Crotalus terr. terr. as described in 1938; at that time only its cystine and methionine contents were quantitatively determined1. This protein, with a molecular weight of 30,0002, proved to be homogeneous3 in the ultra-centrifuge2 as well as by electrophoresis4.
K H, SLOTTA, J, PRIMOSIGH
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Inactivation of crotoxin by group-specific reagents

Biochimica et Biophysica Acta, 1950
Acetylation of most of the amino groups, or esterification of the carboxyl groups of crotoxin causes extensive detoxication. Sulfation of the aliphatic hydroxyl groups, or iodination of most of the phenolic groups, or coupling of these and imidazole groups of the rattlesnake neurotoxin also causes inactivation.
H, FRAENKEL-CONRAT, J, FRAENKEL-CONRAT
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Re-examination of crotoxin-membrane interactions

Toxicon, 1996
The interaction of crotoxin with synaptic membranes from Torpedo marmorata has been re-examined, using radioiodinated toxin. In competition experiments, the 'saturable binding' is usually calculated by subtracting the non-saturable binding, determined in the presence of an excess of unlabelled crotoxin, from total binding.
I, Krizaj, G, Faure, F, Gubensek, C, Bon
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Preparation of a crotoxin neutralizing monoclonal antibody

Toxicon, 1988
Crotoxin is a heterodimeric protein composed of an acidic and basic subunit from the venom of Crotalus durissus terrificus and is representative of a number of presynaptically acting neurotoxins found in the venom of rattlesnakes. Four different monoclonal antibodies, typed as IgG1 subclass, were raised against the basic subunit of this toxin.
I I, Kaiser, J L, Middlebrook
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Crotoxin

2000
Abstract Crotoxin is a dimeric polypeptide (molecular mass, 23.5 kDa) from the venom of the southern Brazilian rattlesnake (Crotalus durissus terrifi,cus) (8,11). The agent acts pre synaptically at motor nerve terminals. In isolated nerve muscle preparations, its effect on transmitter release occurs in three stages (2): An initial ...
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Activation of crotoxin B by volvatoxin A2

Biochemical and Biophysical Research Communications, 1976
Abstract Of the two proteins making up volvatoxin, a mushroom toxin, the smaller, volvatoxin A2, of molecular weight 25,000, is able to synergistically increase the low neurotoxicity of crotoxin B, the larger basic component of the Crotalus durissus terrificus neurotoxin, crotoxin.
T W, Jeng, H, Fraenkel-Conrat
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