메뉴 건너뛰기




Volumn 45, Issue 3, 1997, Pages 639-643

Effect of Chemical Modifications of Phaseolus vulgaris Lectins on Their Biological Properties

Author keywords

Chemical modifications; Lectins; Phaseolus vulgaris; Proteins

Indexed keywords

PHASEOLUS VULGARIS;

EID: 0000852467     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf9600622     Document Type: Article
Times cited : (10)

References (40)
  • 1
    • 0022424797 scopus 로고
    • Binding of isolectins from red kidney bean (Phaseolus vulgaris) to purified rat brush-border membranes
    • Boldt, D. H.; Banwell, J. G. Binding of isolectins from red kidney bean (Phaseolus vulgaris) to purified rat brush-border membranes. Biochim. Biophys. Acta 1985, 843, 230-237.
    • (1985) Biochim. Biophys. Acta , vol.843 , pp. 230-237
    • Boldt, D.H.1    Banwell, J.G.2
  • 3
    • 4444368426 scopus 로고
    • Method for assay of intestinal disaccharidases
    • Dahlqvist, A. Method for assay of intestinal disaccharidases. Anal. Biochem. 1964, 7, 18-25.
    • (1964) Anal. Biochem. , vol.7 , pp. 18-25
    • Dahlqvist, A.1
  • 4
    • 0021268582 scopus 로고
    • Influence of chemical modification and low temperature on the biological properties of Vicia faba lectin
    • Datta, P. K.; Basu, P. S.; Datta, T. K. Influence of chemical modification and low temperature on the biological properties of Vicia faba lectin. IRCS Med Sci. 1984, 12, 687-688.
    • (1984) IRCS Med Sci. , vol.12 , pp. 687-688
    • Datta, P.K.1    Basu, P.S.2    Datta, T.K.3
  • 5
    • 0027133994 scopus 로고
    • Chemical modification and sugar binding properties of two major lectins from pinhão (Araucaria brasiliensis) seeds
    • Datta, P. K.; Figueroa, M. O. R.; Lajolo, F. M. Chemical modification and sugar binding properties of two major lectins from pinhão (Araucaria brasiliensis) seeds, J. Agric. Food Chem. 1993, 41, 1851-1855.
    • (1993) J. Agric. Food Chem. , vol.41 , pp. 1851-1855
    • Datta, P.K.1    Figueroa, M.O.R.2    Lajolo, F.M.3
  • 6
    • 78651153791 scopus 로고
    • Disc electrophoresis. II. Method and application to human serum proteins
    • Davis, B. J. Disc electrophoresis. II. Method and application to human serum proteins. Ann. N.Y. Acad. Sci. 1964, 121, 404-427.
    • (1964) Ann. N.Y. Acad. Sci. , vol.121 , pp. 404-427
    • Davis, B.J.1
  • 7
    • 0039400866 scopus 로고
    • Studies on the modification of soybean agglutinin
    • Desal, N. N.; Alien, A. K.; Neuberger, A. Studies on the modification of soybean agglutinin. Carbohydr. Res. 1988, 178, 183-190.
    • (1988) Carbohydr. Res. , vol.178 , pp. 183-190
    • Desal, N.N.1    Alien, A.K.2    Neuberger, A.3
  • 8
    • 0023283726 scopus 로고
    • Chemical modification of proteins: Comments and perspectives
    • Feeney, R. E. Chemical modification of proteins: comments and perspectives. Int. J. Pept. Protein Res. 1987, 29, 145-161.
    • (1987) Int. J. Pept. Protein Res. , vol.29 , pp. 145-161
    • Feeney, R.E.1
  • 9
    • 0016818858 scopus 로고
    • Purification of the phytohaemagglutinin family of proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatogrphy
    • Felsted, R. L.; Leavitt, R. D.; Bachur, N. R. Purification of the phytohaemagglutinin family of proteins from red kidney beans (Phaseolus vulgaris) by affinity chromatogrphy. Biochim. Biophys. Acta 1975, 405, 73-81.
    • (1975) Biochim. Biophys. Acta , vol.405 , pp. 73-81
    • Felsted, R.L.1    Leavitt, R.D.2    Bachur, N.R.3
  • 10
    • 0017409676 scopus 로고
    • Recombination of subunits of Phaseolus vulgaris isolectins
    • Felsted, R. L.; Egorin, M. J.; Leavitt, R. D.; Bachur, N. R. Recombination of subunits of Phaseolus vulgaris isolectins. J. Biol. Chem. 1977, 252, 2967-2971.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2967-2971
    • Felsted, R.L.1    Egorin, M.J.2    Leavitt, R.D.3    Bachur, N.R.4
  • 11
    • 77957004481 scopus 로고
    • The rapid determination of amino groups with TNBS
    • Fields, R. The rapid determination of amino groups with TNBS. Methods Enzymol. 1972, 25, 464-468.
    • (1972) Methods Enzymol. , vol.25 , pp. 464-468
    • Fields, R.1
  • 12
    • 0021483316 scopus 로고
    • Ação antinutricional das fitohemaglutininas de Phaseolus vulgaris
    • Figueroa, M. O. R.; Mancini, J.; Lajolo, F. M. Ação antinutricional das fitohemaglutininas de Phaseolus vulgaris. Arch. Latinoam. Nutr. 1984, 34, 488-499.
    • (1984) Arch. Latinoam. Nutr. , vol.34 , pp. 488-499
    • Figueroa, M.O.R.1    Mancini, J.2    Lajolo, F.M.3
  • 13
    • 0042524714 scopus 로고
    • Methods for investigating the essential groups for enzyme activity
    • Fraenkel-Conrat, H. Methods for investigating the essential groups for enzyme activity. Methods Enzymol. 1957, 4, 247-269.
    • (1957) Methods Enzymol. , vol.4 , pp. 247-269
    • Fraenkel-Conrat, H.1
  • 14
    • 0014133603 scopus 로고
    • Quantitation of conformational changes on chemical modification of proteins: Use of succinylated protein as a model
    • Habeeb, A. F. S. A. Quantitation of conformational changes on chemical modification of proteins: use of succinylated protein as a model. Arch. Biochem. Biophys. 1967, 121, 652-664.
    • (1967) Arch. Biochem. Biophys. , vol.121 , pp. 652-664
    • Habeeb, A.F.S.A.1
  • 15
    • 0020473052 scopus 로고
    • Mitogenic leucoagglutinin from Phaseolus vulgaris binds to a pentasaccharide unit in N-acetyl-lactosamine-type glycoprotein glycans
    • Hammarstrom, S.; Hammarstrom, M-L.; Sundblad, G.; Arnarp, J.; Lonngreen, J. Mitogenic leucoagglutinin from Phaseolus vulgaris binds to a pentasaccharide unit in N-acetyl-lactosamine-type glycoprotein glycans. Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 1611-1615.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1611-1615
    • Hammarstrom, S.1    Hammarstrom, M.-L.2    Sundblad, G.3    Arnarp, J.4    Lonngreen, J.5
  • 16
    • 0015518513 scopus 로고
    • Further chemical modification studies on concanavalin A, the carbohydrate binding protein of the Jack bean
    • Hassing, G. S.; Goldstein, I. J. Further chemical modification studies on concanavalin A, the carbohydrate binding protein of the Jack bean. Biochim. Biophys. Acta 1972, 271, 388-399.
    • (1972) Biochim. Biophys. Acta , vol.271 , pp. 388-399
    • Hassing, G.S.1    Goldstein, I.J.2
  • 17
    • 0020409906 scopus 로고
    • Kidney bean (Phaseolus vulgaris) lectin induced lesions in rat small intestine
    • King, T. P.; Pusztai, A.; Clarke, E. M. W. Kidney bean (Phaseolus vulgaris) lectin induced lesions in rat small intestine. J. Comp. Pathol. 1982, 92, 357-373.
    • (1982) J. Comp. Pathol. , vol.92 , pp. 357-373
    • King, T.P.1    Pusztai, A.2    Clarke, E.M.W.3
  • 19
    • 0011053560 scopus 로고
    • Chemical modification of the soybean hemagglutinin
    • Liener, I. E.; Wada, S. Chemical modification of the soybean hemagglutinin. J. Biol. Chem. 1956, 222, 695-704.
    • (1956) J. Biol. Chem. , vol.222 , pp. 695-704
    • Liener, I.E.1    Wada, S.2
  • 21
    • 0022555853 scopus 로고
    • Lectins as molecules and tools
    • Lis, H.; Sharon, N. Lectins as molecules and tools. Annu. Rev. Biochem. 1986, 55, 35-67.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 35-67
    • Lis, H.1    Sharon, N.2
  • 23
    • 0001298173 scopus 로고
    • Purification and characterization of a lectin from Phaseolus vulgaris
    • Moreira, R. de A.; Perrone, J. C. Purification and characterization of a lectin from Phaseolus vulgaris. Plant Physiol. 1977, 59, 783-787.
    • (1977) Plant Physiol. , vol.59 , pp. 783-787
    • Moreira, R.D.A.1    Perrone, J.C.2
  • 24
    • 0014518015 scopus 로고
    • Studies on the properties of chemically modified actin. III. Carbethoxylation
    • Mühlrad, A.; Heggi, G.; Horányi, M. Studies on the properties of chemically modified actin. III. Carbethoxylation. Biochim. Biophys. Acta 1969, 181, 184-190.
    • (1969) Biochim. Biophys. Acta , vol.181 , pp. 184-190
    • Mühlrad, A.1    Heggi, G.2    Horányi, M.3
  • 25
    • 0025175234 scopus 로고
    • Binding of tomato lectin to the intestine mucosa and its potential for oral drug delivery
    • Naisbett, B.; Woodley, J. Binding of tomato lectin to the intestine mucosa and its potential for oral drug delivery. Biochem. Soc. Trans. 1990, 18, 879-882.
    • (1990) Biochem. Soc. Trans. , vol.18 , pp. 879-882
    • Naisbett, B.1    Woodley, J.2
  • 26
    • 0000844246 scopus 로고
    • Spectrophotometric determination of histidine in proteins with diethylpyrocarbonate
    • Ovádi, J.; Libor, S.; Elödi, P. Spectrophotometric determination of histidine in proteins with diethylpyrocarbonate. Acta Biochim. Biophys. Acad. Sci. Hung. 1967, 2, 455-458.
    • (1967) Acta Biochim. Biophys. Acad. Sci. Hung. , vol.2 , pp. 455-458
    • Ovádi, J.1    Libor, S.2    Elödi, P.3
  • 27
    • 0016651874 scopus 로고
    • Reversible modification of arginine residues
    • Patthy, L.; Smith, E. L. Reversible modification of arginine residues. J. Biol. Chem. 1975, 250, 557-564.
    • (1975) J. Biol. Chem. , vol.250 , pp. 557-564
    • Patthy, L.1    Smith, E.L.2
  • 28
    • 0023467471 scopus 로고
    • Plant lectins. Biological functions
    • Pusztai, A. Plant lectins. Biological functions. Acta Biochim. Biophys. Hung. 1987, 22, 355-375.
    • (1987) Acta Biochim. Biophys. Hung. , vol.22 , pp. 355-375
    • Pusztai, A.1
  • 29
    • 0016195214 scopus 로고
    • Isolectins of Phaeolus vulgaris. A comprehensive study of fractionation
    • Pusztai, A.; Watt, W. B. Isolectins of Phaeolus vulgaris. A comprehensive study of fractionation. Biochim. Biophys. Acta 1974, 365, 57-71.
    • (1974) Biochim. Biophys. Acta , vol.365 , pp. 57-71
    • Pusztai, A.1    Watt, W.B.2
  • 30
    • 0019627515 scopus 로고
    • The toxicity of Phaseolus vulgaris lectins. Nitrogen balance and immunochemical studies
    • Pusztai, A.; Clarke, E. M. W.; Grant, G.; King, T. P. The toxicity of Phaseolus vulgaris lectins. Nitrogen balance and immunochemical studies. J. Sci. Food Agric. 1981, 32, 1037-1046.
    • (1981) J. Sci. Food Agric. , vol.32 , pp. 1037-1046
    • Pusztai, A.1    Clarke, E.M.W.2    Grant, G.3    King, T.P.4
  • 32
    • 0001412989 scopus 로고
    • Specific uptake of dietary lectins into the systemic circulation of rat
    • Pusztai, A.; Greer, F.; Grant, G. Specific uptake of dietary lectins into the systemic circulation of rat. Biochem. Soc. Trans. 1989, 17, 481-482.
    • (1989) Biochem. Soc. Trans. , vol.17 , pp. 481-482
    • Pusztai, A.1    Greer, F.2    Grant, G.3
  • 33
    • 0025024844 scopus 로고
    • Relationship between survival and binding of plant lectins during small intestinal passage and their effectiveness as growth factors
    • Pusztai, A.; Ewen, S. W. B.; Grant, G.; Peumans, W. J.; Damme, E. J. M. van; Rubio, L.; Nardocz, S. Relationship between survival and binding of plant lectins during small intestinal passage and their effectiveness as growth factors. Digestion 1990, 46 (Suppl. 2), 308-316.
    • (1990) Digestion , vol.46 , Issue.2 SUPPL. , pp. 308-316
    • Pusztai, A.1    Ewen, S.W.B.2    Grant, G.3    Peumans, W.J.4    Van Damme, E.J.M.5    Rubio, L.6    Nardocz, S.7
  • 34
    • 0016719793 scopus 로고
    • Chemical modification and hybridization of wheat germ agglutinins
    • Rice, R. H.; Etzler, M. E. Chemical modification and hybridization of wheat germ agglutinins. Biochemistry 1975, 14, 4903-4909.
    • (1975) Biochemistry , vol.14 , pp. 4903-4909
    • Rice, R.H.1    Etzler, M.E.2
  • 36
    • 0023926631 scopus 로고
    • Selective effects of PHA on rat brush border hydrolases along the crypt-villus axis
    • Rouanet, J. M.; Lafont, J.; Zambonino-Infante, J. L.; Besançon, P. Selective effects of PHA on rat brush border hydrolases along the crypt-villus axis. Experientia 1988, 44, 340-341.
    • (1988) Experientia , vol.44 , pp. 340-341
    • Rouanet, J.M.1    Lafont, J.2    Zambonino-Infante, J.L.3    Besançon, P.4
  • 37
    • 0027158038 scopus 로고
    • Lectin-carbohydrate complexes of plants and animals: An atomic view
    • Sharon, N. Lectin-carbohydrate complexes of plants and animals: an atomic view. Trends Biochem. Sci. 1993, 18, 221-226.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 221-226
    • Sharon, N.1
  • 38
    • 77956994950 scopus 로고
    • Determination of the tryptophan content of proteins with N- bromosuccinimide
    • Spande, T. F.; Witkop, B. Determination of the tryptophan content of proteins with N- bromosuccinimide. Methods Enzymol. 1967, 11, 498-506.
    • (1967) Methods Enzymol. , vol.11 , pp. 498-506
    • Spande, T.F.1    Witkop, B.2
  • 39
    • 0642314535 scopus 로고
    • Chemical modifications of tryptophan residues in Castor bean hemagglutinin
    • Yamasaki, N.; Absar, N.; Funatsu, G. Chemical modifications of tryptophan residues in Castor bean hemagglutinin. Agric. Biol. Chem. 1985, 49, 3301-3308.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 3301-3308
    • Yamasaki, N.1    Absar, N.2    Funatsu, G.3
  • 40
    • 0021112907 scopus 로고
    • Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides
    • Yamashita, K.; Hitoi, A.; Kobata, A. Structural determinants of Phaseolus vulgaris erythroagglutinating lectin for oligosaccharides. J. Biol. Chem. 1983, 258, 14753-14755.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14753-14755
    • Yamashita, K.1    Hitoi, A.2    Kobata, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.