title: Affinity of mutarotase for Sephadex and glycogen.
abstract: It was found that hog kidney mutarotase has an affinity for Sephadex G-100, equilibrated and eluted with 5 mmol/l EDTA buffer (pH 7.4), resulting in retardation of its elution from the column. The affinity was reduced depending upon the presence of 0.15 mol/l NaCl and 0.2 mol/l glucose, separately or in combination. A small portion of mutarotase was adsorbed to rabbit liver glycogen as judged from the column chromatography of a mixture of the two on Bio-Gel P-100. Mutarotase was adsorbed to neither dextran nor raw potato starch.
mesh_terms: D000818:Animals; D002238:Carbohydrate Epimerases / Q000302:isolation & purification*; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D003911:Dextrans; D006003:Glycogen; D007668:Kidney / Q000201:enzymology; D008970:Molecular Weight; D013552:Swine
chemical_list: D003911:Dextrans; D006003:Glycogen; C025614:sephadex; D002238:Carbohydrate Epimerases; C019646:aldose 1-epimerase