Results 151 to 160 of about 1,795 (192)

GSBS News, Summer 2000 [PDF]

open access: yes, 2000
Graduate School of Biomedical Sciences, University of Texas Health Science Center at Houston/M.D. Anderson Cancer Center
core  

Potential of Venom-Derived Compounds for the Development of New Antimicrobial Agents. [PDF]

open access: yesToxins (Basel)
Rabea EY   +10 more
europepmc   +1 more source

Snake venom bioprospecting as an approach to finding potential anti-glioblastoma molecules. [PDF]

open access: yesJ Venom Anim Toxins Incl Trop Dis
Orozco-Mera J   +3 more
europepmc   +1 more source

Molecular Mechanisms of Venom Diversity. [PDF]

open access: yesToxins (Basel)
Ishihara MA, Lopes AR, Nishiyama-Jr MY.
europepmc   +1 more source
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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   +2 more
openaire   +2 more sources

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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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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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
openaire   +2 more sources

The mechanism of inhibition of phospholipase activity of crotoxin B by crotoxin A

Toxicon, 1983
In the crotoxin complex isolated from Crotalus durissus terrificus venom, the component A inhibits the phospholipase A2 activity of crotoxin B only when the substrate is in the aggregated form, preventing the interaction of the enzyme with lecithin--water interfaces.
G, Canziani, C, Seki, J C, Vidal
openaire   +2 more sources

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