Work

Wheat Germ Agglutinin

Year: 1972

Type: article

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.

Source: Journal of Biological Chemistry

DOI: 10.1016/s0021-9258(19)45522-1

Authors: Yoshiho Nagata, Max M. Burger

Institution: Princeton University

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: hybrid

Estimated APC paid: $3,430

OpenAlex ID: W1504713675

FWCI: 7.192

Cites: 13

Cited by: 112

Related to: 10