Chromatography of Glutenin on Sepharose CL-4B in Dissociating Solvents: Molecular Weight Composition of Covalently Bonded Glutenin'

نویسنده

  • S. N. NIGAM
چکیده

Recently we reported that removal of noncovalently bonded protein from glutenin resulted in decreased viscoelasticity. In that study, two glutenin fractions were isolated by successive gel filtration of glutenin on Sephadex G-200 in the solvents acetic acid-guanidine hydrochloride (GuHCl)-cetyltrimethylammonium bromide (AGC) and sodium dodecyl sulfate (SDS). This note reports the S20,W values of these glutenin fractions, and the results of chromatography of glutenin on Sepharose CL-4B in the solvents AGC and SDS. Because of its higher fractionation range over Sephadex G-200, Sepharose CL-4B was used to obtain the information on the molecular weight composition of the covalently bonded glutenin.

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تاریخ انتشار 2005