of human erythrocyte ghosts were solubilized with 0.5yc Triton X-100 in 56 mM sodium borate, pH 8.0. This procedure solubilized 51% of the membrane protein, 81% of the sialic acid, 89% of the receptors for the Agaricus bisporus lectin and 70 to 75% of the wheat germ agglutinin and Ricinus communis lectin receptors. The solubilized glycoproteins were then separated by affinity chromatography on ...

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...

The glycoproteins of plasma membranes from axenically grown Dictyostelium discoideum and human red blood cells (O+) were characterized according to their apparent molecular weights in sodium dodecyl sulfate-polyacrylamide gels and their ability to bind lectins. This was achieved by diffusing each of several fluorescein-conjugated lectins into sodium dodecyl sulfate-polyacrylamide gels which con...

Total nucleic acid extraction and selection of poly A-containing molecules yield preparative quantities of undegraded mRNA from adult and fetal pancreas. Using a stringent immunoassay, this mRNA is found to direct the synthesis of an immunoreactive insulin polypeptide in the wheat germ translation system. On sodium dodecyl sulfate polyacrylamide gels, this polypeptide (12,000-13,000 daltons) is...

Guanine, queuine-tRNA transglycosylase has been purified from wheat germ to homogeneity. The specific activity is 2,000 pmol h-1 mg-1 of protein. The enzyme has an apparent Mr = 140,000. It migrates as a single band with Mr = 68,000 on electrophoresis in sodium dodecyl sulfate gels, indicating two Mr = 68,000 subunits. Both guanine (Km = 6.0 X 10(-8) M) and queuine (KI = 9.5 X 10(-8) M) are sub...

Wheat (Triticum aestivum) RNA was used to program synthesis of the alpha-amylase protein by Xenopus laevis oocytes. A 41,500-dalton protein was made which was identified as alpha-amylase by immunoprecipitation with rabbit anti-alpha-amylase antiserum raised against the purified wheat protein and by its co-migration with authentic alpha-amylase on sodium dodecyl sulfate polyacrylamide gels. Synt...

Turnip Yellow Mosaic Virus RNA directs the synthesis in vitro of its coat protein in a wheat germ cell-free extract. Optimum conditions for synthesis have been defined, and the effect of spermine on specifically enhancing coat protein formation has been examined. Identity between the in vitro synthesized coat protein and authentic coat protein of Turnip Yellow Mosaic Virus was established by an...

We report the purification to apparent homogeneity of an active opioid-binding protein solubilized from bovine striatal membranes. The purification was accomplished in two steps: affinity chromatography on beta-naltrexylethylenediamine (NED)-CH-Sepharose 4B followed by lectin affinity chromatography on wheat germ agglutinin-agarose. The ligand affinity-purified fraction exhibits stereospecific ...

We have identified a yeast protein that resembles actins from other eucaryotes in its tight binding to pancreatic deoxyribonuclease I, its copolymerizaton with purified muscle actin, its one-dimensional peptide map, and its apparent polymerization into 7-nm filaments. The yeast actin-like protein yielded a single spot on two-dimensional polyacrylamide gel electrophoresis, suggesting that a sing...

A factor that binds Met-tRNAF’ in a ternary complex (eucaryotic initiation factor (eIF2)) and an auxiliary component that strongly stimulates the activity of the binding factor (CoeIF2) have been purified from extracts of wheat germ. The molecular weights of the two factors, as determined by glycerol gradient centrifugation and sodium dodecyl sulfate gel electrophoresis, are 88,000 and 20,000, ...