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Original Articles

Etude des interactions in vitro entre les lectines et les glycoprotéines des graines de Légumineuses, à l'aide de lectines marquées à l'isothiocyanate de fluorescéine

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Pages 311-318 | Received 21 Feb 1980, Accepted 18 Apr 1980, Published online: 10 Jul 2014

BIBLIOGRAPHIE

  • AGRAWAL. (B.B.L.) et. GOLDSTEIN (I.J.), 1967.—Protein-carbohydrate interaction. VI. Isolation of Concanavalin A by specific adsorption on cross- linked dextran gels. Biochim. Biophys. Acta, 147, 262–271.
  • BARKER (R.D.J.), DERBYSHIRE (E.), YARWOOD (A.) et BOULTER (D.), 1976.—Purification and characterization of the major storage proteins of Phaseolus vulgaris seeds, and their intracellular and cotyledonary distribution. Phytochem., 15, 751–757.
  • BASHA (S.M.M.) et BEEVERS (L.), 1976.—Glycoprotein metabolism in the cotyledons of Pisum sativum during development and germination. Plant Physiol., 57, 93–97.
  • BASHA (S.M.M.), 1979.—Are lectins of legume seeds involved in cross-linking storage proteins? Plant Physiol., 63, Suppl. 5, Abstract 324, 59.
  • BOLLINI (R.) et CHRISPEELS (M.J.), 1978.—Characterization and subcellular localization of vicilin and phytohemagglutinin. the two major reserve proteins of Phaseolus vulgaris L. Planta, 142, 291–298.
  • CHRAMBACH (A.), REISFELD (R.A.), WYCKOFF (M.) et ZACCARI (J.), 1967.—A procedure for rapid and sensitive staining of protein fractionated by polyacrylamide gel electrophoresis. Analyt. Biochem., 20, 1–15.
  • CLARKE (A.E.), KNOX (R.B. et JERMYN (M.A.), 1975.—Localization of lectins in legume cotyledons. J. Cell. Sci., 19, 157–167.
  • DAVIS (B.J.), 1964.—Disc electrophoresis. II. Method and application to human serum proteins. Ann. N. Y. Aced. Sc., 121, 404–427.
  • ERICSON (M.E.) et CHRISPEELS (M.J.), 1973.—Isolation and characterization of glucosamine containing storage glycoproteins from the cotyledons of Phaseolus aureus. Plant Physiol., 52, 98–104.
  • FURLAN (M.), PERRET (B.A.) et BECK (E.A.), 1979.—Staining of glycoprotein in Polyacrylamide and agarose gels with fluorescent lectins. Analyt. Biochem., 96, 208–214.
  • JACKSON (P.), BOULTER (D.) et THURMAN (D.A.), 1969.—A comparison of some properties of vicilin and legumin isolated from seeds of Pisum sativum, Vicia faba and Cicer arietinum. New Phytol., 68, 25–33.
  • KILPATRICK (D.C.), YEOMAN (M.M.) et GOULD (A.R.), 1979.—Tissue and subcellular distribution of the lectin from Datura stramonium (Thorn apple). Biochem. J., 184, 215–219.
  • MIALONIER (G.). PRIVAT (J.P.), MONSIGNY (M.). KAHLEM (G.) et DURAND (R.), 1973.—Isolement, propriétés physico-chimiques et localisation in vivo d'une phytohémagglutinine (lectine) de Phaseolus vulgaris L. (var. rouge). Physiol, vég., 11, 519–537.
  • PUSZTAI (A.) et WATT (W.B.). 1970.—Glycoprotein II. The isolation and characterization of a major antigenic and non-haemagglutinating glycoprotein from Phaseolus vulgaris. Biochim. Biophys. Acta, 207, 413–431.
  • PUSZTAI (A.), CROY (R.R.D.) et WATT (W.B.), 1977.—Compartmentalization in the cotyledonary cells of Phaseolus vulgaris L. seeds: a differential sedimentation study. New Phytol., 79, 61–71.
  • RAGUSEN (D.) et FOOTE (M.), 1971.—The major glycoprotein in germinating bean seeds. Can. J. Bot., 49, 2107–2111.
  • ROUGÉ (P.), 1977.—Biologie des hémagglutinines chez le Pois (Pisum sativum L.). Thèse Doct. ès-Sc., Toulouse.
  • ROUGÉ (P.) et PÈRE (M.), 1979.—Etude des interactions entre les lectines et les constituants glueidiques (glycoprotéines et glucides solubles) des graines de quelques Légumineuses. Bull. Soc. bot. Fr., 126, 387–398.
  • THE (T.H.) et FELTKAMP (T.E.W.), 1970.—Conjugation of fluorescein isothiocyanate to antibodies. I. Experiments on the conditions of conjugation. Immunology, 18, 865–873.
  • TULLY (R.E.) et BEEVERS (H.), 1976.—Protein bodies of castor bean endosperm. Isolation, fractionation, and the characterization of protein components. Plant Physiol., 58, 710–716.
  • YOULE (R.J.) et HUANG (A.H.C.), 1976. Protein bodies from the endosperm of castor bean. Subfradionation. protein components, lectins, and changes during germination. Plant Physiol; 58. 703–709.

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