The purification and characterization of wheat-germ agglutinin
نویسندگان
چکیده
منابع مشابه
The purification and characterization of wheat-germ agglutinin.
The purification of wheat-germ agglutinin by precipitation with ammonium sulphate and by chromatography on Sephadex G-75, Sepharose-ovomucoid and CM-cellulose is described. This procedure gave agglutinin preparations which were homogeneous on polyacrylamide gels under a variety of conditions. Purified wheat-germ agglutinin formed colourless solutions and was relatively insoluble at neutral pH; ...
متن کاملWheat 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...
متن کاملMechanism of neutrophil chemiluminescence induced by wheat germ agglutinin: partial characterization of the antigens recognized by wheat germ agglutinin.
Wheat germ agglutinin (WGA) stimulated neutrophils to produce significant levels of luminol-dependent chemiluminescence (CL). Since WGA is known to bind N-acetylglucosamine (GlcNAc) oligomers and N-acetylneuraminic acid (NANA), we attempted to determine which binding property of WGA is essential for induction of CL. The succinylated form of WGA (SuWGA), which is no longer able to bind NANA, was...
متن کاملImmunocytochemical localization of wheat germ agglutinin in wheat
Immunocytological techniques were developed to localize the plant lectin, wheat germ agglutinin (WGA), in the tissues and cells of wheat plants. In a previous study we demonstrated with a radioimmunoassay that the lectin is present in wheat embryos and adult plants both in the roots and at the base of the stem. We have now found, using rhodamine, peroxidase, and ferritin-labeled secondary antib...
متن کاملPurification and characterization of a wheat germ protein kinase.
A cyclic AMP-independent protein kinase has been purified from wheat germ extracts. The enzyme catalyzes the phosphorylation of casein and phosvitin but not protamine, histone, or bovine serum albumin. However, the best substrate for the kinase appears to be that of an endogenous wheat germ protein. The kinase can utilize both ATP and GTP as phosphoryl donors. A molecular weight of 36,000-38,00...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Biochemical Journal
سال: 1972
ISSN: 0306-3283
DOI: 10.1042/bj1290847