Folding and Homodimerization of Wheat Germ Agglutinin

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Wheat Germ Agglutinin

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...

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ژورنال

عنوان ژورنال: Biophysical Journal

سال: 2011

ISSN: 0006-3495

DOI: 10.1016/j.bpj.2011.07.037