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Purification of 21-kDa protein. 10 mg of venom was separated by <t>Q-Sepharose</t> ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.
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Purification of 21-kDa protein. 10 mg of venom was separated by Q-Sepharose ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.

Journal: The Journal of Biological Chemistry

Article Title: Rhinocetin, a Venom-derived Integrin-specific Antagonist Inhibits Collagen-induced Platelet and Endothelial Cell Functions *

doi: 10.1074/jbc.M112.381483

Figure Lengend Snippet: Purification of 21-kDa protein. 10 mg of venom was separated by Q-Sepharose ion-exchange chromatography ( A ), and the selected fractions (9–26) were analyzed by 10% non-reducing SDS-PAGE ( B ). The partially purified protein at 21 kDa is indicated by arrows . Selected fractions were further separated by Superdex 75 gel filtration chromatography ( C ) and analyzed by 10% non-reducing SDS-PAGE ( D ). The purified venom protein was analyzed under non-reducing and reducing conditions by 4–20% gradient SDS-PAGE ( E ) and 10–20% Tris-Tricine gels ( F ). The cross-reactivity of antibody raised against the snaclecs of E. ocellatus with the purified protein was analyzed by immunoblot (obtained from a Tris-Tricine gel under non-reducing ( left ) and reducing ( right ) conditions) ( G ). mAU , milliabsorbance units; MW , molecular weight.

Article Snippet: The clear venom sample was loaded on to a 1-ml prepacked Q-Sepharose anion-exchange column (GE Healthcare).

Techniques: Purification, Ion Exchange Chromatography, SDS Page, Filtration, Chromatography, Western Blot, Molecular Weight