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Acid phosphatase and proteinase activities of selected crotalid venoms.
SAAS bulletin, biochemistry and biotechnology, 1996 C A, Sifford, D H, Sifford, B D, Johnson
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Toxicon, 1988
The binding of Antivenom (Crotalidae) Polyvalent to fractions from crude venoms of eight crotalid and one viperid snake, obtained by high performance size-exclusion chromatography, was determined with an indirect enzyme-linked immunosorbent assay (ELISA). Most of the large (greater than 30,000 mol.
R C, Schaeffer +3 more
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The binding of Antivenom (Crotalidae) Polyvalent to fractions from crude venoms of eight crotalid and one viperid snake, obtained by high performance size-exclusion chromatography, was determined with an indirect enzyme-linked immunosorbent assay (ELISA). Most of the large (greater than 30,000 mol.
R C, Schaeffer +3 more
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Antigenic relatedness of crotalid venoms: The basic subunit of mojave toxin
Toxicon, 1985 openaire +2 more sources
Toxicon, 1985
We have developed a simple two-step procedure for the separation of monomeric (14,000 mol. wt) and dimeric (28,000 mol. wt) phospholipases A2 from the venoms of Crotalidae family snakes. All venom phospholipases A2 studied thus far exist as monomers under acidic conditions and are chromatographed as such on a column of G-50 Sephadex (superfine ...
W, Welches +3 more
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We have developed a simple two-step procedure for the separation of monomeric (14,000 mol. wt) and dimeric (28,000 mol. wt) phospholipases A2 from the venoms of Crotalidae family snakes. All venom phospholipases A2 studied thus far exist as monomers under acidic conditions and are chromatographed as such on a column of G-50 Sephadex (superfine ...
W, Welches +3 more
openaire +2 more sources