메뉴 건너뛰기




Volumn 20, Issue 5, 2013, Pages 499-509

Purification and biophysical characterization of an 11s globulin from wrightia tinctoria exhibiting hemagglutinating activity

Author keywords

11S globulin; Apocynaceae; Hemagglutinating activity; Wrightia tinctoria

Indexed keywords

COMPLEMENTARY DNA; GLOBULIN; LECTIN; MESSENGER RNA;

EID: 84877990144     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/0929866511320050002     Document Type: Article
Times cited : (5)

References (63)
  • 1
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: Structures, properties and role in grain utilization
    • Shewry, P.R.; Halford, N.G. Cereal seed storage proteins: structures, properties and role in grain utilization. J. Exp. Bot., 2002, 53(370), 947-958.
    • (2002) J. Exp. Bot , vol.53 , Issue.370 , pp. 947-958
    • Shewry, P.R.1    Halford, N.G.2
  • 2
    • 0000711035 scopus 로고    scopus 로고
    • Seed storage proteins and approaches for improvement of their nutritional quality by genetic engineering
    • Mandal, S.; Mandal, R.K. Seed storage proteins and approaches for improvement of their nutritional quality by genetic engineering. Curr. Sci., 2000, 79(5), 576-589.
    • (2000) Curr. Sci , vol.79 , Issue.5 , pp. 576-589
    • Mandal, S.1    Mandal, R.K.2
  • 3
    • 0041833728 scopus 로고    scopus 로고
    • Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate
    • Rangel, A.; Domont, G.B.; Pedrosa, C.; Ferreira, S.T. Functional properties of purified vicilins from cowpea (Vigna unguiculata) and pea (Pisum sativum) and cowpea protein isolate. J. Agric. Food. Chem., 2003, 51(19), 5792-5797.
    • (2003) J. Agric. Food. Chem , vol.51 , Issue.19 , pp. 5792-5797
    • Rangel, A.1    Domont, G.B.2    Pedrosa, C.3    Ferreira, S.T.4
  • 4
    • 0016187789 scopus 로고
    • Purification and subunit structure of legumin of Vicia faba L. (broad bean)
    • Wright, D.J.; Boulter, D. Purification and subunit structure of legumin of Vicia faba L. (broad bean). Biochem. J., 1974, 141(2), 413-418.
    • (1974) Biochem. J , vol.141 , Issue.2 , pp. 413-418
    • Wright, D.J.1    Boulter, D.2
  • 5
    • 0000800863 scopus 로고    scopus 로고
    • Biochemical characterization of soybean protein consisting of different subunits of glycinin
    • Yagasaki, K.; Takagi, T.; Sakai, M.; Kitamura, K. Biochemical characterization of soybean protein consisting of different subunits of glycinin. J. Agric. Food Chem., 1997, 45(3), 656-660.
    • (1997) J. Agric. Food Chem , vol.45 , Issue.3 , pp. 656-660
    • Yagasaki, K.1    Takagi, T.2    Sakai, M.3    Kitamura, K.4
  • 7
    • 33749531916 scopus 로고    scopus 로고
    • The interaction of the 11S globulin-like protein of kiwifruit seeds with pepsin
    • Rassam, M.; Laing, W.A. The interaction of the 11S globulin-like protein of kiwifruit seeds with pepsin. J. Plant Sci., 2006, 171(6), 663-669.
    • (2006) J. Plant Sci , vol.171 , Issue.6 , pp. 663-669
    • Rassam, M.1    Laing, W.A.2
  • 8
    • 0000374202 scopus 로고
    • Identification of homologous globulins from embryos of wheat, barley, rye and oats
    • Burgess, S.R.; Shewry, P.R. Identification of homologous globulins from embryos of wheat, barley, rye and oats. J. Exp. Bot., 1986, 37(12), 1863-1871.
    • (1986) J. Exp. Bot , vol.37 , Issue.12 , pp. 1863-1871
    • Burgess, S.R.1    Shewry, P.R.2
  • 9
    • 0026940188 scopus 로고
    • Rice seed globulin: A protein similar to wheat seed glutenin
    • Komatsu, S.; Hirano, H. Rice seed globulin: a protein similar to wheat seed glutenin. Phytochem., 1992, 31(10), 3455-3459.
    • (1992) Phytochem , vol.31 , Issue.10 , pp. 3455-3459
    • Komatsu, S.1    Hirano, H.2
  • 10
    • 46949105561 scopus 로고    scopus 로고
    • Crystallization and initial crystallographic characterization of the Ginkgo biloba 11S seed globulin ginnacin. Acta Crystallogr
    • Jin, T.; Chen, Y.W.; Howard, A.; Zhang, Y.Z. Purification, crystallization and initial crystallographic characterization of the Ginkgo biloba 11S seed globulin ginnacin. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 2008, 64(7), 641-644.
    • (2008) Sect. F Struct. Biol. Cryst. Commun , vol.64 , Issue.7 , pp. 641-644
    • Jin, T.1    Chen, Y.W.2    Howard, A.3    Purification, Z.Z.Y.4
  • 11
    • 77949348558 scopus 로고    scopus 로고
    • Purification of legumin-like proteins from Coffea arabica and Coffea racemosa seeds and their insecticidal properties toward cowpea weevil (Callosobruchus maculatus)( Coleoptera: Bruchidae
    • Coelho, M.B.; Macedo, M.L.R.; Marangoni, S.; Silva, D.S.; Cesarino, I.; Mazzafera, P. Purification of legumin-like proteins from Coffea arabica and Coffea racemosa seeds and their insecticidal properties toward cowpea weevil (Callosobruchus maculatus)( Coleoptera: Bruchidae). J. Agric. Food Chem., 2010, 58(5), 3050-3055.
    • (2010) J. Agric. Food Chem , vol.58 , Issue.5 , pp. 3050-3055
    • Coelho, M.B.1    MacEdo, M.L.R.2    Marangoni, S.3    Silva, D.S.4    Cesarino, I.5    Mazzafera, P.6
  • 13
    • 37549056273 scopus 로고    scopus 로고
    • Purification identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis
    • Gaur, V.; Sethi, D.K.; Salunke, D.M. Purification, identification and preliminary crystallographic studies of Pru du amandin, an allergenic protein from Prunus dulcis. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 2008, 64(1), 32-35.
    • (2008) Acta Crystallogr Sect. F Struct. Biol. Cryst. Commun , vol.64 , Issue.1 , pp. 32-35
    • Gaur, V.1    Sethi, D.K.2    Salunke, D.M.3
  • 14
    • 0036740044 scopus 로고    scopus 로고
    • Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions
    • Beyer, K.; Grishina, G.; Bardina, L.; Grishin, A.; Sampson, H.A. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J. Allergy Clin. Immunol., 2002, 110(3), 517-23.
    • (2002) J. Allergy Clin. Immunol , vol.110 , Issue.3 , pp. 517-523
    • Beyer, K.1    Grishina, G.2    Bardina, L.3    Grishin, A.4    Sampson, H.A.5
  • 15
    • 0348237005 scopus 로고    scopus 로고
    • Effect of a toxic protein isolated from Zea mays seeds on the development and survival of the cowpea weevil, Callosobruchus maculatus
    • Macedo, M.L.R.; Coelho, M.B.; Freire, M.G.M.; Machado, O.L.T.; Marangoni, S.; Novello, J.C. Effect of a toxic protein isolated from Zea mays seeds on the development and survival of the cowpea weevil, Callosobruchus maculatus. Protein Pept. Lett., 2000, 7(4), 225-232.
    • (2000) Protein Pept. Lett , vol.7 , Issue.4 , pp. 225-232
    • MacEdo, M.L.R.1    Coelho, M.B.2    Freire, M.G.M.3    MacHado, O.L.T.4    Marangoni, S.5    Novello, J.C.6
  • 16
    • 34547883567 scopus 로고    scopus 로고
    • Characterization and insecticidal properties of globulins and albumins from Luetzelburgia auriculata (Allemao) Ducke seeds towards Callosobruchus maculatus (F.)(Coleoptera: Bruchidae)
    • Soares, E.L.; Freitas, C.D.T.; Oliveira, J.S.; Sousa, P.A.S.; Sales, M.P.; Barreto-Filho, J.D.M.; Bandeira, G.P.; Ramos, M.V. Characterization and insecticidal properties of globulins and albumins from Luetzelburgia auriculata (Allemao) Ducke seeds towards Callosobruchus maculatus (F.)(Coleoptera: Bruchidae). J. Stored Prod. Res., 2007, 43(4), 459-467.
    • (2007) J. Stored Prod. Res , vol.43 , Issue.4 , pp. 459-467
    • Soares, E.L.1    Freitas, C.D.T.2    Oliveira, J.S.3    Sousa, P.A.S.4    Sales, M.P.5    Barreto-Filho, J.D.M.6    Bandeira, G.P.7    Ramos, M.V.8
  • 17
    • 34047218362 scopus 로고    scopus 로고
    • Effects of a chitin-binding vicilin from Enterolobium contortisiliquum seeds on bean bruchid pests (Callosobruchus maculatus and Zabrotes subfasciatus) and phytopathogenic fungi (Fusarium solani and Colletrichum lindemuntianum
    • Moura, F.T.; Oliveira, A.S.; Macedo, L.L.P.; Vianna, A.L.B.R.; Andrade, L.B.S.; Martins-Miranda, A.S.; Oliveira, J.T.A.; Santos, E.A.; Mauricio, P. Effects of a chitin-binding vicilin from Enterolobium contortisiliquum seeds on bean bruchid pests (Callosobruchus maculatus and Zabrotes subfasciatus) and phytopathogenic fungi (Fusarium solani and Colletrichum lindemuntianum). J. Agric. Food Chem., 2007, 55(2), 260-266.
    • (2007) J. Agric. Food Chem , vol.55 , Issue.2 , pp. 260-266
    • Moura, F.T.1    Oliveira, A.S.2    MacEdo, L.L.P.3    Vianna, A.L.B.R.4    Andrade, L.B.S.5    Martins-Miranda, A.S.6    Oliveira, J.T.A.7    Santos, E.A.8    Mauricio, P.9
  • 18
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • Shewry, P.R.; Napier, J.A.; Tatham, A.S. Seed storage proteins: structures and biosynthesis. Plant Cell, 1995, 7(7), 945-956.
    • (1995) Plant Cell , vol.7 , Issue.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 19
    • 70349314612 scopus 로고    scopus 로고
    • Crystal structure of prunin-1, a major component of the almond (Prunus dulcis) allergen amandin
    • Jin, T.A.; Albillos, S.M.; Guo, F.; Howard, A.; Fu, T.J.; Kothary, M.H.; Zhang, Y.Z. Crystal structure of prunin-1, a major component of the almond (Prunus dulcis) allergen amandin. J. Agric. Food Chem., 2009, 57(18), 8643-8651.
    • (2009) J. Agric. Food Chem , vol.57 , Issue.18 , pp. 8643-8651
    • Jin, T.A.1    Albillos, S.M.2    Guo, F.3    Howard, A.4    Fu, T.J.5    Kothary, M.H.6    Zhang, Y.Z.7
  • 20
    • 0042303912 scopus 로고    scopus 로고
    • Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S
    • Adachi, M.; Okuda, E.; Kaneda, Y.; Hashimoto, A.; Shutov, A. D.; Becker, C.; Mntz, K.; Utsumi, S., Crystal structures and structural stabilities of the disulfide bond-deficient soybean proglycinin mutants C12G and C88S. J. Agric. Food Chem., 2003, 51(16), 4633-4639.
    • (2003) J. Agric. Food Chem , vol.51 , Issue.16 , pp. 4633-4639
    • Adachi, M.1    Okuda, E.2    Kaneda, Y.3    Hashimoto, A.4    Shutov, A.D.5    Becker, C.6    Mntz, K.7    Utsumi, S.8
  • 22
    • 0001064980 scopus 로고    scopus 로고
    • Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds
    • Mntz, K. Proteases and proteolytic cleavage of storage proteins in developing and germinating dicotyledonous seeds. J. Exp. Bot., 1996, 47(5), 605-622.
    • (1996) J. Exp. Bot , vol.47 , Issue.5 , pp. 605-622
    • Mntz, K.1
  • 24
    • 0037164030 scopus 로고    scopus 로고
    • Lectins and protease inhibitors as plant defenses against insects
    • Murdock, L.L.; Shade, R.E. Lectins and protease inhibitors as plant defenses against insects. J. Agric. Food. Chem., 2002, 50(22), 6605-6611.
    • (2002) J. Agric. Food. Chem , vol.50 , Issue.22 , pp. 6605-6611
    • Murdock, L.L.1    Shade, R.E.2
  • 28
    • 0000476634 scopus 로고
    • A revision of the genus Wrightia (Apocynaceae
    • Ngan, P.T. A revision of the genus Wrightia (Apocynaceae). Ann. Missouri Bot. Gard., 1965, 52(2), 114-175.
    • (1965) Ann. Missouri Bot. Gard , vol.52 , Issue.2 , pp. 114-175
    • Ngan, P.T.1
  • 30
    • 77957789242 scopus 로고    scopus 로고
    • Vitro antifungal activity of indirubin isolated from a South Indian ethnomedicinal plant Wrightia tinctoria
    • Ponnusamy, K.; Petchiammal, C.; Mohankumar, R.; Hopper, W. In vitro antifungal activity of indirubin isolated from a South Indian ethnomedicinal plant Wrightia tinctoria R. Br. J. Ethnopharmacol., 2010, 132(1), 349-354.
    • (2010) R. Br. J. Ethnopharmacol. , vol.132 , Issue.1 , pp. 349-354
    • Ponnusamy, K.1    Petchiammal, C.2    Mohankumar, R.3    Hopper, W.4
  • 32
    • 84869113776 scopus 로고    scopus 로고
    • Anti oxidation activity of Wrightia tinctoria Roxb bark and Schrebera swietenoides Roxb bark extract
    • Kumar, L.; Rao, K.N.V.; Madhvi, b.; Kumar, S.; Banji, D. Anti oxidation activity of Wrightia tinctoria Roxb bark and Schrebera swietenoides Roxb bark extract. J. Pharm. Res., 2011, 4(2), 396-397.
    • (2011) J. Pharm. Res. , vol.4 , Issue.2 , pp. 396-397
    • Kumar, L.1    Rao, K.N.V.2    Madhvi, B.3    Kumar, S.4    Banji, D.5
  • 33
    • 84855677467 scopus 로고    scopus 로고
    • Pharmacognostical and physicochemical standardization of ethnopharmacologically important seeds of Lepidium sativum Linn. and Wrightia tinctoria
    • Bigoniya, P.; Singh, C.S.; Shukla, A. Pharmacognostical and physicochemical standardization of ethnopharmacologically important seeds of Lepidium sativum Linn. and Wrightia tinctoria R. Br. Indian J. Nat. Prod. Resour., 2011, 2(4), 464-471.
    • (2011) R. Br. Indian J. Nat. Prod. Resour. , vol.2 , Issue.4 , pp. 464-471
    • Bigoniya, P.1    Singh, C.S.2    Shukla, A.3
  • 34
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 1970, 227(5259), 680-685.
    • (1970) Nature , vol.227 , Issue.5259 , pp. 680-685
    • Laemmli, U.K.1
  • 35
    • 0023664635 scopus 로고
    • Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes
    • Matsudaira, P. Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem., 1987, 262(21), 10035-10038.
    • (1987) J. Biol. Chem , vol.262 , Issue.21 , pp. 10035-10038
    • Matsudaira, P.1
  • 36
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis
    • Rosenfeld, J.; Capdevielle, J.; Guillemot, J.C.; Ferrara, P. In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis. Anal. Biochem., 1992, 203(1), 173-179.
    • (1992) Anal. Biochem , vol.203 , Issue.1 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 37
    • 33745842211 scopus 로고    scopus 로고
    • Evaluation of chemical derivatisation methods for protein identification using MALDI MS/MS
    • Joss, J.L.; Molloy, M.P.; Hinds, L.A.; Deane, E.M. Evaluation of chemical derivatisation methods for protein identification using MALDI MS/MS. Int. J. Pept. Res. Ther., 2006, 12(3), 225-235.
    • (2006) Int. J. Pept. Res. Ther , vol.12 , Issue.3 , pp. 225-235
    • Joss, J.L.1    Molloy, M.P.2    Hinds, L.A.3    Deane, E.M.4
  • 38
    • 0001298173 scopus 로고
    • Purification and partial characterization of a lectin from Phaseolus vulgaris
    • Moreira, R.D.A.; Perrone, J.C. Purification and partial characterization of a lectin from Phaseolus vulgaris. Plant Physiol., 1977, 59(5), 783.
    • (1977) Plant Physiol , vol.59 , Issue.5 , pp. 783
    • Moreira, R.D.A.1    Perrone, J.C.2
  • 39
    • 0035574823 scopus 로고    scopus 로고
    • Isolation and partial characterization of a lectin from Bauhinia pentandra (bong) vog. Ex. Steua
    • Horta, A.N.A.C.G.; De Azevedo, M.R. Isolation and partial characterization of a lectin from Bauhinia pentandra (bong) vog. Ex. Steua. Braz. J. Plant Physiol., 2001, 13(3), 262.
    • (2001) Braz. J. Plant Physiol , vol.13 , Issue.3 , pp. 262
    • Horta, A.N.A.C.G.1    De Azevedo, M.R.2
  • 40
    • 24544447317 scopus 로고
    • Heat-Induced gel formation of- lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy
    • Matsuura, J.E.; Manning, M.C. Heat-Induced gel formation of- lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem., 1994, 42(8), 1650-1656.
    • (1994) J. Agric. Food Chem , vol.42 , Issue.8 , pp. 1650-1656
    • Matsuura, J.E.1    Manning, M.C.2
  • 42
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • Whitmore, L.; Wallace, B.A. DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res., 2004, 32(suppl 2), W668-W673.
    • (2004) Nucleic Acids Res , vol.32 , Issue.SUPPL. 2
    • Whitmore, L.1    Wallace, B.A.2
  • 43
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Macromolecular Crystallography, Part A
    • Otwinowski, Z.; Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol., 1997, 276(Macromolecular Crystallography, Part A), 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 44
    • 0028103275 scopus 로고
    • Programs for protein crystallography
    • CCP4, Collaborative Computational Project Number 4, The CCP4 Suite
    • CCP4, Collaborative Computational Project Number 4, The CCP4 Suite: Programs for Protein Crystallography. Acta Crystallogr. D Biol. Crystallogr. 1994, 50(1), 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , Issue.1 , pp. 760-763
  • 45
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: An automated program for molecular replacement
    • Vagin, A.; Teplyakov, A., MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr., 1997, 30(6), 1022-1025.
    • (1997) J. Appl. Crystallogr , vol.30 , Issue.6 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 46
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P.; Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr., 2004, 60(12), 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr , vol.60 , Issue.12 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 47
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G.N.; Vagin, A.A.; Dodson, E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D Biol. Crystallogr., 1997, 53(3), 240-255.
    • (1997) Acta Crystallogr. D Biol. Crystallogr , vol.53 , Issue.3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 48
    • 0020210720 scopus 로고
    • Separation and characterization of oat globulin polypeptides
    • Brinegar, A.C.; Peterson, D.M. Separation and characterization of oat globulin polypeptides. Arch. Biochem. Biophys., 1982, 219(1), 71-79.
    • (1982) Arch. Biochem. Biophys , vol.219 , Issue.1 , pp. 71-79
    • Brinegar, A.C.1    Peterson, D.M.2
  • 49
    • 0000646051 scopus 로고
    • Subunit structure and composition of oat seed globulin
    • Peterson, D.M. Subunit structure and composition of oat seed globulin. Plant physiol., 1978, 62(4), 506-509.
    • (1978) Plant Physiol , vol.62 , Issue.4 , pp. 506-509
    • Peterson, D.M.1
  • 50
    • 84966154541 scopus 로고
    • Genetic variability in the structure of the-subunits of legumin from Pisum-A two-dimensional gel electrophoresis study
    • Casey, R. Genetic variability in the structure of the-subunits of legumin from Pisum-A two-dimensional gel electrophoresis study. Heredity, 1979, 43(2), 265-272.
    • (1979) Heredity , vol.43 , Issue.2 , pp. 265-272
    • Casey, R.1
  • 51
    • 84861438673 scopus 로고
    • A seed storage protein with possible self-affinity through lectin-like binding
    • Langston-Unkefer, P.J.; Gade, W. A seed storage protein with possible self-affinity through lectin-like binding. Plant physiol., 1984, 74(3), 675-680.
    • (1984) Plant Physiol , vol.74 , Issue.3 , pp. 675-680
    • Langston-Unkefer, P.J.1    Gade, W.2
  • 52
    • 33748697399 scopus 로고    scopus 로고
    • Purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds
    • Choi, S.M.; Ma, C.Y. Extraction, purification and characterization of globulin from common buckwheat (Fagopyrum esculentum Moench) seeds. Food Res. Intl., 2006, 39(9), 974-981.
    • (2006) Food Res. Intl , vol.39 , Issue.9 , pp. 974-981
    • Choi, S.M.1    Extraction, Y.M.C.2
  • 53
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen, Y.; Barkley, M.D. Toward understanding tryptophan fluorescence in proteins. Biochemistry, 1998, 37(28), 9976-9982.
    • (1998) Biochemistry , vol.37 , Issue.28 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 55
    • 78651077844 scopus 로고    scopus 로고
    • Lectins: Production and practical applications
    • Lam, S.K.; Ng, T.B. Lectins: production and practical applications. Appl. Microbiol. Biotechnol., 2011, 89(1), 45-55.
    • (2011) Appl. Microbiol. Biotechnol. , vol.89 , Issue.1 , pp. 45-55
    • Lam, S.K.1    Ng, T.B.2
  • 56
    • 79954457401 scopus 로고    scopus 로고
    • Functional alteration of a dimeric insecticidal lectin to a monomeric antifungal protein correlated to its oligomeric status
    • Banerjee, N.; Sengupta, S.; Roy, A.; Ghosh, P.; Das, K.; Das, S. Functional alteration of a dimeric insecticidal lectin to a monomeric antifungal protein correlated to its oligomeric status. PLoS ONE, 2011, 6(4), e18593.
    • (2011) PLoS ONE , vol.6 , Issue.4
    • Banerjee, N.1    Sengupta, S.2    Roy, A.3    Ghosh, P.4    Das, K.5    Das, S.6
  • 57
    • 0000310777 scopus 로고
    • Secondary structure of globulins from plant seeds: A reevaluation from circular dichroism measurements
    • Zirwer, D.; Gast, K.; Welfle, H.; Schlesier, B.; Dieter Schwenke, K. Secondary structure of globulins from plant seeds: A reevaluation from circular dichroism measurements. Int. J. Biol. Macromol., 1985, 7(2), 105-108.
    • (1985) Int. J. Biol. Macromol , vol.7 , Issue.2 , pp. 105-108
    • Zirwer, D.1    Gast, K.2    Welfle, H.3    Schlesier, B.4    Dieter Schwenke, K.5
  • 58
    • 35548957779 scopus 로고    scopus 로고
    • A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and-conglycinin (7S)
    • Clara Sze, K.W.; Kshirsagar, H.H.; Venkatachalam, M.; Sathe, S.K. A circular dichroism and fluorescence spectrometric assessment of effects of selected chemical denaturants on soybean (Glycine max L.) storage proteins glycinin (11S) and-conglycinin (7S). J. Agric. Food Chem., 2007, 55(21), 8745-8753.
    • (2007) J. Agric. Food Chem , vol.55 , Issue.21 , pp. 8745-8753
    • Clara Sze, K.W.1    Kshirsagar, H.H.2    Venkatachalam, M.3    Sathe, S.K.4
  • 59
    • 62549131255 scopus 로고    scopus 로고
    • A novel sialic acid-specific lectin from Phaseolus coccineus seeds with potent antineoplastic and antifungal activities
    • Chen, J.; Liu, B.; Ji, N.; Zhou, J.; Bian, H.; Li, C.; Chen, F.; Bao, J. A novel sialic acid-specific lectin from Phaseolus coccineus seeds with potent antineoplastic and antifungal activities. Phytomedicine, 2009, 16(4), 352-360.
    • (2009) Phytomedicine , vol.16 , Issue.4 , pp. 352-360
    • Chen, J.1    Liu, B.2    Ji, N.3    Zhou, J.4    Bian, H.5    Li, C.6    Chen, F.7    Bao, J.8
  • 60
    • 0028180075 scopus 로고
    • High-pressure effects on- lactoglobulin interactions with ligands studied by fluorescence
    • Dufour, E.; Hoa, G.H.B.; Haertle, T. High-pressure effects on- lactoglobulin interactions with ligands studied by fluorescence. Biochim. Biophys. Acta, 1994, 1206(2), 166-172.
    • (1994) Biochim. Biophys. Acta , vol.1206 , Issue.2 , pp. 166-172
    • Dufour, E.1    Hoa, G.H.B.2    Haertle, T.3
  • 61
    • 77952196858 scopus 로고    scopus 로고
    • Purification and biochemical characterization of Brazil nut (Bertholletia excelsa L.) seed storage proteins
    • Sharma, G.M.; Mundoma, C.; Seavy, M.; Roux, K.H.; Sathe, S.K. Purification and biochemical characterization of Brazil nut (Bertholletia excelsa L.) seed storage proteins. J. Agric. Food Chem., 2010, 58(9), 5714-5723.
    • (2010) J. Agric. Food Chem , vol.58 , Issue.9 , pp. 5714-5723
    • Sharma, G.M.1    Mundoma, C.2    Seavy, M.3    Roux, K.H.4    Sathe, S.K.5
  • 62
    • 78649430650 scopus 로고    scopus 로고
    • Conformational and thermal properties of phaseolin, the major storage protein of red kidney bean (Phaseolus vulgaris L.)
    • Yin, S.W.; Tang, C.H.; Wen, Q.B.; Yang, X.Q. Conformational and thermal properties of phaseolin, the major storage protein of red kidney bean (Phaseolus vulgaris L.). J. Sci. Food Agric., 2011, 91(1), 94-99.
    • (2011) J. Sci. Food Agric. , vol.91 , Issue.1 , pp. 94-99
    • Yin, S.W.1    Tang, C.H.2    Wen, Q.B.3    Yang, X.Q.4
  • 63
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B.W. Solvent content of protein crystals. J. Mol. Biol., 1968, 33(2), 491-497.
    • (1968) J. Mol. Biol , vol.33 , Issue.2 , pp. 491-497
    • Matthews, B.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.