نتایج جستجو برای: wheat germ extract

تعداد نتایج: 264315  

2002
YOSHIHO NAGATA MAX M. BURGER

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...

Journal: :Journal of oleo science 2009
Norihisa Iwamoto Takashi Kobayashi Shuji Adachi

The antioxidative activities of durum wheat flour and its components on linoleic acid were examined at 50 degrees C and 12% relative humidity. The progress of the oxidation was monitored by the pressure change due to the oxygen consumption during the oxidation. The antioxidative capacities were assessed by the length of the induction period for the oxidation. Durum wheat flour and its methanol ...

Journal: :The Plant cell 2007
Naoki Shitsukawa Chikako Tahira Ken-Ichiro Kassai Chizuru Hirabayashi Tomoaki Shimizu Shigeo Takumi Keiichi Mochida Kanako Kawaura Yasunari Ogihara Koji Murai

Bread wheat (Triticum aestivum) is a hexaploid species with A, B, and D ancestral genomes. Most bread wheat genes are present in the genome as triplicated homoeologous genes (homoeologs) derived from the ancestral species. Here, we report that both genetic and epigenetic alterations have occurred in the homoeologs of a wheat class E MADS box gene. Two class E genes are identified in wheat, whea...

Journal: :Nucleic acids research 1978
D Hatfield M Rice

Isoacceptors of Ala-, Arg-, Glu-, Gln-, Ile-, Leu-, Lys-, Ser-, Thr- and Val-tRNAs from wheat germ have been resolved by reverse phast chromatography. Codon recognition properties have been determined on isolated fractions of each of these aa-tRNAs and codon assignments have been made to a number of isoacceptors. Evolutionary changes which have occurred in patterns of codon recognition by isoac...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1977
J L Spivak D Small M D Hollenberg

Affinity chromatography using agarose-bound lectins was used to isolate erythropoietin from crude preparations of sheep plasma and human urinary erythropoietin. On the basis of previous estimates of the sugar content of the hormone, six lectins (wheat germ agglutinin, phytohemagglutinin, Ricinus communis 120, soybean agglutinin, concanavalin A, and limulin) were chosen for study. Only wheat ger...

Journal: :Journal of cell science 1975
R M Rizki T M Rizki C A Andrews

The effects of wheat germ agglutinin on Drosophila embryonic cell lines growing on cover-glasses was examined by scanning electron microscopy. At low concentrations of the lectin (5-10 mug/ml), cells spread against the glass surface and fused to form syncytia. At high concentration, damage to the cell surface was evidenced as extensive membrane shrivelling and loss of surface microfilaments. Fu...

Journal: :Journal of clinical microbiology 1979
R L Schaefer K F Keller R J Doyle

A lectin slide agglutination test has been developed for the confirmatory identification of Neisseria gonorrhoeae. With wheat germ lectin as an agglutinin, 164 of 165 clinical isolates of N. gonorrhoeae gave a 3 to 4+ reaction within 6 to 8 min. Four gonococcal isolates, even though negative by the fluoresecent-antibody method, gave strong positive reactions with the wheat germ lectin. Among 23...

Journal: :The Journal of biological chemistry 1967
F C Stevens A N Glazer E L Smith

Determination of the complete amino acid sequence of wheat germ cytochrome c has shown that the molecule consists of a single polypeptide chain of 112 residues. On alignment with mammalian cytochromes, the peptide chain extends for 8 residues at the NH&erminal end. In contrast with other cytochromes that have a peptide chain longer than 104 residues, the NHt-terminal residue is Nacetylalanine. ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1971
W T Shier

A synthetic antigen containing the presumed receptor site for wheat-germ agglutinin (a lectin capable of specifically agglutinating tumor cells) elicits an immune response in mice capable of cross-reacting with receptor sites for wheat-germ agglutinin on tumor-cell surfaces. Mice immunized against the antigen in complete Freund's adjuvant are able to reject five times as many transplanted myelo...

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