sepharose and ammonium-acetate

sepharose has been researched along with ammonium-acetate* in 1 studies

Other Studies

1 other study(ies) available for sepharose and ammonium-acetate

Article	Year
Isolation of a novel agglutinin with complex carbohydrate binding specificity from fresh fruiting bodies of the edible mushroom Lyophyllum shimeiji. Biochemical and biophysical research communications, 2002, Jan-11, Volume: 290, Issue:1 A hemagglutinin, with a molecular weight of 30,000 and expressing hemagglutinating activity which could not be inhibited by simple sugars and glycoproteins, was isolated from fresh fruiting bodies of the edible mushroom Lyophyllum shimeiji. The protein was adsorbed on CM-Sepharose even in 20 mM ammonium acetate (pH 5.5) containing 1 M NaCl and was desorbed by 20 mM ammonium bicarbonate (pH 9). The hemagglutinating activity was subsequently adsorbed on Mono S in 20 mM ammonium acetate (pH 5.5) and was desorbed by a linear gradient of 0.2-0.5 M NaCl in ammonium acetate buffer. The hemagglutinin exhibited a novel N-terminal sequence not found in any lectin and hemagglutinin reported so far. It was devoid of antifungal activity. Topics: Acetates; Agglutinins; Amino Acid Sequence; Basidiomycota; Carbohydrate Metabolism; Chromatography, Affinity; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Lectins; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Sepharose; Sodium Chloride	2002

Article

Year

Isolation of a novel agglutinin with complex carbohydrate binding specificity from fresh fruiting bodies of the edible mushroom Lyophyllum shimeiji.

Biochemical and biophysical research communications, 2002, Jan-11, Volume: 290, Issue:1

A hemagglutinin, with a molecular weight of 30,000 and expressing hemagglutinating activity which could not be inhibited by simple sugars and glycoproteins, was isolated from fresh fruiting bodies of the edible mushroom Lyophyllum shimeiji. The protein was adsorbed on CM-Sepharose even in 20 mM ammonium acetate (pH 5.5) containing 1 M NaCl and was desorbed by 20 mM ammonium bicarbonate (pH 9). The hemagglutinating activity was subsequently adsorbed on Mono S in 20 mM ammonium acetate (pH 5.5) and was desorbed by a linear gradient of 0.2-0.5 M NaCl in ammonium acetate buffer. The hemagglutinin exhibited a novel N-terminal sequence not found in any lectin and hemagglutinin reported so far. It was devoid of antifungal activity.

Topics: Acetates; Agglutinins; Amino Acid Sequence; Basidiomycota; Carbohydrate Metabolism; Chromatography, Affinity; Chromatography, Ion Exchange; Electrophoresis, Polyacrylamide Gel; Hydrogen-Ion Concentration; Lectins; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Sepharose; Sodium Chloride

2002