Wheat Germ Agglutinin
Yoshiho Nagata(Princeton University), Max M. Burger(Princeton University)
Cited by 112Open Access
Abstract
Abstract 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 agglutinin 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.