Wheat Germ Agglutinin
نویسندگان
چکیده
Procedures for the isolation, purification, and crystallization of wheat germ agglutinin are described. The agglutinin was purified 184-fold to homogeneity from commercial wheat germ lipase. A molecular weight of 23,500 was estimated for the protein by means of sedimentation equilibrium and sodium dodecyl sulfate gel electrophoresis. The agghxtinin is a glycoprotein. Amino acid and carbohydrate compositions are reported. The protein contains unusually high half-cystine and glycine. Glucose was found to be the major carbohydrate constituent.
منابع مشابه
Increase in cell surface wheat germ agglutinin binding in a rat hepatoma cell line dRLa 74 treated with concanavalin A.
Wheat germ agglutinin binding to a rat hepatoma cell line dRLa 74 treated with concanavalin A was studied. It increased depending on the concanavalin A concentration in the culture medium. The cells exhibited about twofold increase in wheat germ agglutinin-binding when pretreated with 50 micrograms/ml of concanavalin A for 48 h. The wheat germ agglutinin binding sites were shown to be localized...
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