Title of article
Elution of tightly bound solutes from concanavalin A Sepharose: Factors affecting the desorption of cottonmouth venom glycoproteins
Author/Authors
Soper، نويسنده , , Anastasiya S. and Aird، نويسنده , , Steven D.، نويسنده ,
Issue Information
روزنامه با شماره پیاپی سال 2007
Pages
11
From page
308
To page
318
Abstract
Some glycoproteins bind so tightly to concanavalin A Sepharose that common desorption techniques are ineffective, so a systematic exploration of factors affecting desorption of cottonmouth venom glycoproteins was undertaken. Glycoprotein desorption is greatly improved by introducing up to four pauses of 5–10 min duration into the elution step. Eluent concentrations above 250 mM methylglucoside or 500 mM methyl-mannoside reduced glycoprotein desorption. Eluent NaCl diminished glycoprotein desorption. Most venom glycoproteins desorb more readily as pH diminishes from 6.0 to 4.0, but phosphodiesterase shows the opposite pattern. Eluents recommended by the supplier for desorbing solutes or for column cleaning were ineffectual.
Keywords
Triton X-100 , Ionic strength , Agkistrodon piscivorus leucostoma venom , affinity chromatography , phosphodiesterase , Lectin , glycoprotein , Methyl-?-d-glucopyranoside , Methyl-?-d-mannopyranoside , Ethylene glycol , Desorption pauses , Concanavalin A Sepharose , PH , urea , Propanol , Ethanol , Nacl
Journal title
Journal of Chromatography A
Serial Year
2007
Journal title
Journal of Chromatography A
Record number
1521874
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