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Graduate School of Biomedical Sciences, University of Texas Health Science Center at Houston/M.D. Anderson Cancer Center
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Potential of Venom-Derived Compounds for the Development of New Antimicrobial Agents. [PDF]
Rabea EY +10 more
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Venom-derived peptides for breaking through the glass ceiling of drug development. [PDF]
Freuville L +3 more
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Snake venom bioprospecting as an approach to finding potential anti-glioblastoma molecules. [PDF]
Orozco-Mera J +3 more
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Molecular Mechanisms of Venom Diversity. [PDF]
Ishihara MA, Lopes AR, Nishiyama-Jr MY.
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The active components of crotoxin
Biochemical and Biophysical Research Communications, 1972Summary 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
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Amino-acid Composition of Crotoxin
Nature, 1951THE 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, 1956Abstract 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, 1982Basic 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 mechanism of inhibition of phospholipase activity of crotoxin B by crotoxin A
Toxicon, 1983In 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
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