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Volumn 104, Issue 3, 2007, Pages 971-979

Isolation and characterization of a lectin with antifungal activity from Egyptian Pisum sativum seeds

Author keywords

Antifungal; Characterization; Hemagglutination activity; Leguminoseae; Mannose binding lectin; Pisum sativum; Purification

Indexed keywords

CALCIUM; LECTIN; MANGANESE; MANNOSE;

EID: 34248582180     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2007.01.026     Document Type: Article
Times cited : (76)

References (37)
  • 1
    • 0034851060 scopus 로고    scopus 로고
    • Mannose-binding plant lectins: different structurl scaffolds for a common sugar-recognition process
    • Barre A., Bourne Y., Van Damme E.J.M., Peamans W.J., and Rouge P. Mannose-binding plant lectins: different structurl scaffolds for a common sugar-recognition process. Biochimie 83 (2001) 645-651
    • (2001) Biochimie , vol.83 , pp. 645-651
    • Barre, A.1    Bourne, Y.2    Van Damme, E.J.M.3    Peamans, W.J.4    Rouge, P.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0002504789 scopus 로고
    • Monosaccharides
    • Chaplin M.F., and Kennedy J.F. (Eds), Oxford University Press, Oxford
    • Chaplin M.F. Monosaccharides. In: Chaplin M.F., and Kennedy J.F. (Eds). Carbohydrate analysis a practical approach (1994), Oxford University Press, Oxford
    • (1994) Carbohydrate analysis a practical approach
    • Chaplin, M.F.1
  • 4
    • 0025718126 scopus 로고
    • Lectins, lectin genes and their role in plant defense
    • Chrispeels M.J., and Raikhel N.V. Lectins, lectin genes and their role in plant defense. Plant Cell 3 (1991) 1-9
    • (1991) Plant Cell , vol.3 , pp. 1-9
    • Chrispeels, M.J.1    Raikhel, N.V.2
  • 8
    • 0017057686 scopus 로고
    • N-Terminal sequences of the α and β subunits of the lectin from the garden pea (Pisum Sativum)
    • Driessche E.V., Foriers A., Stroberg A.D., and Kanarek L. N-Terminal sequences of the α and β subunits of the lectin from the garden pea (Pisum Sativum). Febs Letters 71 (1976) 220-222
    • (1976) Febs Letters , vol.71 , pp. 220-222
    • Driessche, E.V.1    Foriers, A.2    Stroberg, A.D.3    Kanarek, L.4
  • 10
    • 0002199711 scopus 로고
    • Isolation, physicochemical characterization and carbohydrate binding proteins of lectins
    • Liener I.E., Sharon N., and Goldstein I.J. (Eds), Academic Press, Florida
    • Goldstein I.J., and Portez R.D. Isolation, physicochemical characterization and carbohydrate binding proteins of lectins. In: Liener I.E., Sharon N., and Goldstein I.J. (Eds). Lectins properties, functions and applications in biology and medicine (1986), Academic Press, Florida 35-247
    • (1986) Lectins properties, functions and applications in biology and medicine , pp. 35-247
    • Goldstein, I.J.1    Portez, R.D.2
  • 11
    • 0028112288 scopus 로고
    • A survey of antifungal compounds from higher plants
    • Grayer R.J., and Harbone J.B. A survey of antifungal compounds from higher plants. Phytochemistry 37 (1994) 19-42
    • (1994) Phytochemistry , vol.37 , pp. 19-42
    • Grayer, R.J.1    Harbone, J.B.2
  • 12
    • 0033180204 scopus 로고    scopus 로고
    • Some thaumatin-like proteins hydrolyze polymeric B-1,3-glucans
    • Grenier J., Potvin C., Trudel J., and Asselin A. Some thaumatin-like proteins hydrolyze polymeric B-1,3-glucans. Plant Journal 19 (1999) 473-480
    • (1999) Plant Journal , vol.19 , pp. 473-480
    • Grenier, J.1    Potvin, C.2    Trudel, J.3    Asselin, A.4
  • 13
    • 34248595158 scopus 로고
    • Gel filtration
    • Protein purification. Janson J.C., and Ryde L. (Eds), Oxford University Press, Oxford
    • Hagel L. Gel filtration. In: Janson J.C., and Ryde L. (Eds). Protein purification. Principles, high resolution methods, and applications (1994), Oxford University Press, Oxford 79-143
    • (1994) Principles, high resolution methods, and applications , pp. 79-143
    • Hagel, L.1
  • 15
    • 0037443111 scopus 로고    scopus 로고
    • Isolation, purification, and physicohemical characterization of a d-galactose-binding lectin form seeds of Erythrina Speciosa
    • Konozy E.H., Bernardes E.S., Rosa C., Faca V., Greene L.J., and Ward R.J. Isolation, purification, and physicohemical characterization of a d-galactose-binding lectin form seeds of Erythrina Speciosa. Archive of Biochemistry and Biophysics 410 (2003) 222-229
    • (2003) Archive of Biochemistry and Biophysics , vol.410 , pp. 222-229
    • Konozy, E.H.1    Bernardes, E.S.2    Rosa, C.3    Faca, V.4    Greene, L.J.5    Ward, R.J.6
  • 17
    • 11544358874 scopus 로고    scopus 로고
    • Lectins: carbohydrate-specific proteins that mediate cellular recognition
    • Lis H., and Sharon N. Lectins: carbohydrate-specific proteins that mediate cellular recognition. Chemical Reviews 98 (1998) 637-674
    • (1998) Chemical Reviews , vol.98 , pp. 637-674
    • Lis, H.1    Sharon, N.2
  • 18
    • 0037136417 scopus 로고    scopus 로고
    • Principles of structures of animal and plant lectins
    • Loris R. Principles of structures of animal and plant lectins. Biochimica Et Biophysica Acta 1572 (2002) 198-208
    • (2002) Biochimica Et Biophysica Acta , vol.1572 , pp. 198-208
    • Loris, R.1
  • 20
    • 0015953462 scopus 로고
    • Studies on phytohemagglutinins. Xvi. Subunit structure of the pea isophytohemagglutinins
    • Marik R., Entlicher G., and Kocourek J. Studies on phytohemagglutinins. Xvi. Subunit structure of the pea isophytohemagglutinins. Biochimica Et Biophysica Acta 336 (1974) 53-61
    • (1974) Biochimica Et Biophysica Acta , vol.336 , pp. 53-61
    • Marik, R.1    Entlicher, G.2    Kocourek, J.3
  • 22
    • 19744368180 scopus 로고    scopus 로고
    • Characterization of a common intermediate of pea lectin in the folding path way induced by Tfe and Hfip
    • Naseem F., and Khan R.H. Characterization of a common intermediate of pea lectin in the folding path way induced by Tfe and Hfip. Biochimica Et Biophysica Acta 1723 (2005) 192-200
    • (2005) Biochimica Et Biophysica Acta , vol.1723 , pp. 192-200
    • Naseem, F.1    Khan, R.H.2
  • 23
  • 24
    • 0029379651 scopus 로고
    • Lectins as plant defense proteins
    • Peumans W.J., and Van Damme E.M. Lectins as plant defense proteins. Plant Physiology 109 (1995) 347-352
    • (1995) Plant Physiology , vol.109 , pp. 347-352
    • Peumans, W.J.1    Van Damme, E.M.2
  • 25
    • 0027317526 scopus 로고
    • Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins
    • Pusztai A. Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins. British Journal of Nutrition 70 (1993) 313-321
    • (1993) British Journal of Nutrition , vol.70 , pp. 313-321
    • Pusztai, A.1
  • 27
    • 0342529369 scopus 로고
    • Isolation of plant lectins
    • Gabius H.J., and Gabius S. (Eds), Springer Verlag, Berlin
    • Rudiger H. Isolation of plant lectins. In: Gabius H.J., and Gabius S. (Eds). Lectins and Glycobiology (1993), Springer Verlag, Berlin 32-46
    • (1993) Lectins and Glycobiology , pp. 32-46
    • Rudiger, H.1
  • 28
    • 0036703175 scopus 로고    scopus 로고
    • Plant lectins: occurrence, biochemistry, functions and applications
    • Rudiger H., and Gabius H.J. Plant lectins: occurrence, biochemistry, functions and applications. Glycoconjugte Journal 18 (2001) 589-613
    • (2001) Glycoconjugte Journal , vol.18 , pp. 589-613
    • Rudiger, H.1    Gabius, H.J.2
  • 29
    • 0027538064 scopus 로고
    • Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum Sativum) lectin, and lentil (Lens Culinaris) lectin
    • Schwarz F.P., Puri K.D., Bhat R.G., and Surolia A. Thermodynamics of monosaccharide binding to concanavalin A, pea (Pisum Sativum) lectin, and lentil (Lens Culinaris) lectin. Journal of Biological Chemistry 268 (1993) 7668-7677
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 7668-7677
    • Schwarz, F.P.1    Puri, K.D.2    Bhat, R.G.3    Surolia, A.4
  • 30
    • 0037164098 scopus 로고    scopus 로고
    • How proteins bind carbohydrte: lessons from legume lectins
    • Sharon N., and Lis H. How proteins bind carbohydrte: lessons from legume lectins. Journal of Agriculture and Food Chemistry 50 (2002) 6586-6591
    • (2002) Journal of Agriculture and Food Chemistry , vol.50 , pp. 6586-6591
    • Sharon, N.1    Lis, H.2
  • 31
    • 0035882421 scopus 로고    scopus 로고
    • Legume lectin family the natural mutants of the quaternary state provide insights into the relationship between protein stability and oligimerization
    • Srinivas V.R., Reddy G.B., Ahmad N., Swaminathan C.P., Mitra N., Surolia A., et al. Legume lectin family the natural mutants of the quaternary state provide insights into the relationship between protein stability and oligimerization. Biochimica Et Biophysica Acta 1527 (2001) 102-111
    • (2001) Biochimica Et Biophysica Acta , vol.1527 , pp. 102-111
    • Srinivas, V.R.1    Reddy, G.B.2    Ahmad, N.3    Swaminathan, C.P.4    Mitra, N.5    Surolia, A.6
  • 32
    • 0029163653 scopus 로고
    • Purification of a lectin from Parkia Javanica beans
    • Utarabhand P., and Akkayamount P. Purification of a lectin from Parkia Javanica beans. Phytochemistry 38 (1995) 281-285
    • (1995) Phytochemistry , vol.38 , pp. 281-285
    • Utarabhand, P.1    Akkayamount, P.2
  • 33
    • 0032422738 scopus 로고    scopus 로고
    • Plant lectins: a composite of several distinct families of structurally devolutionary related proteins with diverse biological roles
    • Van Damme E.J.M., Van Damme W., Prumans W.J., Barre A., and Rouge P. Plant lectins: a composite of several distinct families of structurally devolutionary related proteins with diverse biological roles. Critical Reviews in Plant Sciences 17 (1998) 575-692
    • (1998) Critical Reviews in Plant Sciences , vol.17 , pp. 575-692
    • Van Damme, E.J.M.1    Van Damme, W.2    Prumans, W.J.3    Barre, A.4    Rouge, P.5
  • 34
  • 35
    • 0034762513 scopus 로고    scopus 로고
    • Isolation of a homodimeric lectin with antifungal and antiviral activites from red kidney bean (Phaseolus Valgaris) seeds
    • Ye X.Y., Ng T.B., Tsang P.W., and Wang J. Isolation of a homodimeric lectin with antifungal and antiviral activites from red kidney bean (Phaseolus Valgaris) seeds. Journal of Protein Chemistry 20 (2001) 367-375
    • (2001) Journal of Protein Chemistry , vol.20 , pp. 367-375
    • Ye, X.Y.1    Ng, T.B.2    Tsang, P.W.3    Wang, J.4
  • 36
    • 0034762513 scopus 로고    scopus 로고
    • Isolation of a homodimeric lectin with antifungal and antiviral activities from red kidney bean (Phaseolus Vulgaris) seeds
    • Ye X.Y., Ng T.B., Tsang P.W.K., and Wang J. Isolation of a homodimeric lectin with antifungal and antiviral activities from red kidney bean (Phaseolus Vulgaris) seeds. Journal of Protein Chemistry 20 (2001) 367-375
    • (2001) Journal of Protein Chemistry , vol.20 , pp. 367-375
    • Ye, X.Y.1    Ng, T.B.2    Tsang, P.W.K.3    Wang, J.4
  • 37
    • 0032059804 scopus 로고    scopus 로고
    • Osmotin a plant antifungal protein subverts signal transudation to enhance fungal cell susceptibility
    • Yun D.J., Ibeas J.I., Lee H., Coca M.A., Narasimham M.L., and Uesono Y. Osmotin a plant antifungal protein subverts signal transudation to enhance fungal cell susceptibility. Mollecular Cell 1 (1998) 807-817
    • (1998) Mollecular Cell , vol.1 , pp. 807-817
    • Yun, D.J.1    Ibeas, J.I.2    Lee, H.3    Coca, M.A.4    Narasimham, M.L.5    Uesono, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.