메뉴 건너뛰기




Volumn 323, Issue 2, 2004, Pages 484-490

Protection of Mucuna pruriens seeds against Echis carinatus venom is exerted through a multiform glycoprotein whose oligosaccharide chains are functional in this role

Author keywords

2 D gel electrophoresis; Carbohydrate epitopes; Glycoproteins; N linked oligosaccharides; Plant extract; Snake venom

Indexed keywords

ALKALI; AMINO ACID; ANTIBODY; ANTIGEN; ASPARTYLASPARTYLARGINYLGLUTAMYLPROLYLVALYLASPARTYLTHREONINE; CONCANAVALIN A; GLYCAN; GLYCOPROTEIN; MUCUNA PRURIENS EXTRACT; OLIGOSACCHARIDE; PLANT EXTRACT; PROTEIN; SNAKE VENOM; SOYBEAN TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 4544233271     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.08.122     Document Type: Article
Times cited : (36)

References (30)
  • 2
    • 0035238881 scopus 로고    scopus 로고
    • Plants as source of drugs
    • S.M.K. Rates Plants as source of drugs Toxicon 39 2001 603 613
    • (2001) Toxicon , vol.39 , pp. 603-613
    • Rates, S.M.K.1
  • 3
    • 0031831843 scopus 로고    scopus 로고
    • Adjuvant effects and antiserum action potentiation by a (herbal) compound 2-hydroxy-4-methoxy benzoic acid isolated from the root extract of the Indian medicinal plant 'sarsaparilla' (Hemidesmus indicus R. Br.)
    • M.I. Alam, and A. Gomes Adjuvant effects and antiserum action potentiation by a (herbal) compound 2-hydroxy-4-methoxy benzoic acid isolated from the root extract of the Indian medicinal plant 'sarsaparilla' (Hemidesmus indicus R. Br.) Toxicon 36 1998 1423 1431
    • (1998) Toxicon , vol.36 , pp. 1423-1431
    • Alam, M.I.1    Gomes, A.2
  • 5
    • 0034735974 scopus 로고    scopus 로고
    • Plant natural products active against snake biteâ€"the molecular approach
    • W.B. Mors, M.C. Nascimento, B.M. Pereira, and N.A. Pereira Plant natural products active against snake biteâ€"the molecular approach Phytochemistry 55 2000 627 642
    • (2000) Phytochemistry , vol.55 , pp. 627-642
    • Mors, W.B.1    Nascimento, M.C.2    Pereira, B.M.3    Pereira, N.A.4
  • 6
    • 0036661358 scopus 로고    scopus 로고
    • Ethnomedical knowledge of plants used by Kunabi Tribe of Karnataka in India
    • V.H. Harsha, S.S. Hebbar, G.R. Hegde, and V. Shripathi Ethnomedical knowledge of plants used by Kunabi Tribe of Karnataka in India Fitoterapia 73 2002 281 287
    • (2002) Fitoterapia , vol.73 , pp. 281-287
    • Harsha, V.H.1    Hebbar, S.S.2    Hegde, G.R.3    Shripathi, V.4
  • 7
    • 0035999663 scopus 로고    scopus 로고
    • Medical ethnobotany of the tribals of Sonaghati of Sonbhadra district, Uttar Pradesh, India
    • A.K. Singh, A.S. Raghubanshi, and J.S. Singh Medical ethnobotany of the tribals of Sonaghati of Sonbhadra district, Uttar Pradesh, India J. Ethnopharmacol. 81 2002 31 41
    • (2002) J. Ethnopharmacol. , vol.81 , pp. 31-41
    • Singh, A.K.1    Raghubanshi, A.S.2    Singh, J.S.3
  • 8
    • 0036943741 scopus 로고    scopus 로고
    • Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera
    • M. Deepa, and V.T. Gowda Purification and characterization of a glycoprotein inhibitor of toxic phospholipase from Withania somnifera Arch. Biochem. Biophys. 408 2002 42 50
    • (2002) Arch. Biochem. Biophys. , vol.408 , pp. 42-50
    • Deepa, M.1    Gowda, V.T.2
  • 9
    • 0026597190 scopus 로고
    • Studies on chemical composition and antinutritional factors in three germplasm seed materials of the tribal pulse, Mucuna pruriens (L.) DC
    • R.M. Josephine, and K. Janardhanan Studies on chemical composition and antinutritional factors in three germplasm seed materials of the tribal pulse, Mucuna pruriens (L.) DC Food Chem. 43 1992 13 18
    • (1992) Food Chem. , vol.43 , pp. 13-18
    • Josephine, R.M.1    Janardhanan, K.2
  • 10
    • 0035070378 scopus 로고    scopus 로고
    • Effects of Mucuna pruriens extract on activation of prothrombin by Echis carinatus venom
    • R. Guerranti, J.C. Aguiyi, E. Errico, R. Pagani, and E. Marinello Effects of Mucuna pruriens extract on activation of prothrombin by Echis carinatus venom J. Ethnopharmacol. 75 2001 175 180
    • (2001) J. Ethnopharmacol. , vol.75 , pp. 175-180
    • Guerranti, R.1    Aguiyi, J.C.2    Errico, E.3    Pagani, R.4    Marinello, E.5
  • 11
    • 0032952891 scopus 로고    scopus 로고
    • Studies on possible protection against snake venom using Mucuna pruriens protein immunization
    • J.C. Aguiyi, A.C. Igweh, U.G. Egesie, and R. Leoncini Studies on possible protection against snake venom using Mucuna pruriens protein immunization Fitoterapia 70 1999 21 24
    • (1999) Fitoterapia , vol.70 , pp. 21-24
    • Aguiyi, J.C.1    Igweh, A.C.2    Egesie, U.G.3    Leoncini, R.4
  • 12
    • 0037053321 scopus 로고    scopus 로고
    • Proteins from Mucuna pruriens and enzymes from Echis carinatus venom: Characterization and cross-reactions
    • R. Guerranti, J.C. Aguiyi, S. Neri, R. Leoncini, R. Pagani, and E. Marinello Proteins from Mucuna pruriens and enzymes from Echis carinatus venom: characterization and cross-reactions J. Biol. Chem. 277 2002 17072 17078
    • (2002) J. Biol. Chem. , vol.277 , pp. 17072-17078
    • Guerranti, R.1    Aguiyi, J.C.2    Neri, S.3    Leoncini, R.4    Pagani, R.5    Marinello, E.6
  • 13
    • 0026801909 scopus 로고
    • Plant with a reputation against snakebite
    • W. Martz Plant with a reputation against snakebite Toxicon 30 1992 1131 1142
    • (1992) Toxicon , vol.30 , pp. 1131-1142
    • Martz, W.1
  • 15
    • 0035667032 scopus 로고    scopus 로고
    • Blood chemistry of rats pretreated with Mucuna pruriens seed aqueous extract MP101UJ after Echis carinatus venom challenge
    • J.C. Aguiyi, R. Guerranti, R. Pagani, and E. Marinello Blood chemistry of rats pretreated with Mucuna pruriens seed aqueous extract MP101UJ after Echis carinatus venom challenge Phytother. Res. 15 2001 712 714
    • (2001) Phytother. Res. , vol.15 , pp. 712-714
    • Aguiyi, J.C.1    Guerranti, R.2    Pagani, R.3    Marinello, E.4
  • 16
    • 0036816556 scopus 로고    scopus 로고
    • Glycosylation of proteins in plants and invertebrates
    • I.B. Wilson Glycosylation of proteins in plants and invertebrates Curr. Opin. Struct. Biol. 12 2002 569 577
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 569-577
    • Wilson, I.B.1
  • 18
    • 0035958916 scopus 로고    scopus 로고
    • Identification of core alpha 1, 3-fucosylatedglycans glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the anti-horseadish peroxidase epitope
    • G. Fabini, A. Freilinger, F. Altmann, and I.B.H. Wilson Identification of core alpha 1, 3-fucosylatedglycans glycans and cloning of the requisite fucosyltransferase cDNA from Drosophila melanogaster. Potential basis of the anti-horseadish peroxidase epitope J. Biol. Chem. 276 2001 28058 28067
    • (2001) J. Biol. Chem. , vol.276 , pp. 28058-28067
    • Fabini, G.1    Freilinger, A.2    Altmann, F.3    Wilson, I.B.H.4
  • 19
    • 0026691179 scopus 로고
    • The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. the role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine
    • C. Prenner, L. Mach, J. Glossl, and L. Marz The antigenicity of the carbohydrate moiety of an insect glycoprotein, honey-bee (Apis mellifera) venom phospholipase A2. The role of alpha 1,3-fucosylation of the asparagine-bound N-acetylglucosamine Biochem. J. 284 1992 377 380
    • (1992) Biochem. J. , vol.284 , pp. 377-380
    • Prenner, C.1    MacH, L.2    Glossl, J.3    Marz, L.4
  • 20
    • 0023886064 scopus 로고
    • The presence of non-isotope specific antibodies in polyclonal anti IgE reagents: Demonstration of their binding to specific selected Epsteinâ€"Barr virus transformed cell lines
    • M. Steinitz, S. Tamir, S.B. Sela, and E. Rosenmann The presence of non-isotope specific antibodies in polyclonal anti IgE reagents: demonstration of their binding to specific selected Epsteinâ€"Barr virus transformed cell lines Cell. Immunol. 113 1988 10 19
    • (1988) Cell. Immunol. , vol.113 , pp. 10-19
    • Steinitz, M.1    Tamir, S.2    Sela, S.B.3    Rosenmann, E.4
  • 21
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 23
    • 0023768475 scopus 로고
    • Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): The state of the art and the controversy of vertical versus horizontal systems
    • A. Görg Two-dimensional polyacrylamide gel electrophoresis with immobilized pH gradients in the first dimension (IPG-Dalt): the state of the art and the controversy of vertical versus horizontal systems Electrophoresis 9 1988 531 546
    • (1988) Electrophoresis , vol.9 , pp. 531-546
    • Görg, A.1
  • 24
    • 0021189137 scopus 로고
    • Demonstration of peptide: N-glycosidase F activity in endo-β-N-acetylglucosaminidase F preparations
    • T.H. Plummer Jr., J.H. Elder, S. Alexander, A.W. Phelan, and A.L. Tarentino Demonstration of peptide: N-glycosidase F activity in endo-β-N-acetylglucosaminidase F preparations J. Biol. Chem. 259 1984 10700 10704
    • (1984) J. Biol. Chem. , vol.259 , pp. 10700-10704
    • Plummer Jr., T.H.1    Elder, J.H.2    Alexander, S.3    Phelan, A.W.4    Tarentino, A.L.5
  • 25
    • 0028875728 scopus 로고
    • Active site and oligosaccharide recognition residues of peptide-N4-(N-acetyl-beta-d-glucosaminyl) asparagine amidase F
    • P. Kuhn, C. Guan, T. Cui, A.L. Tarentino, T.H. Plummer Jr., and P. Van Roey Active site and oligosaccharide recognition residues of peptide-N4-(N-acetyl-beta-d-glucosaminyl) asparagine amidase F J. Biol. Chem. 270 1995 29493 29497
    • (1995) J. Biol. Chem. , vol.270 , pp. 29493-29497
    • Kuhn, P.1    Guan, C.2    Cui, T.3    Tarentino, A.L.4    Plummer Jr., T.H.5    Van Roey, P.6
  • 26
    • 0037096068 scopus 로고    scopus 로고
    • Analysis of O-linked reducing oligosaccharides released by an in-line flow system
    • N.G. Karlsson, and N.H. Packer Analysis of O-linked reducing oligosaccharides released by an in-line flow system Anal. Biochem. 305 2002 173 185
    • (2002) Anal. Biochem. , vol.305 , pp. 173-185
    • Karlsson, N.G.1    Packer, N.H.2
  • 27
    • 0033991744 scopus 로고    scopus 로고
    • Characterization of the seed proteins of velvet bean(Mucuna pruriens) from Nigeria
    • J. Machuka Characterization of the seed proteins of velvet bean(Mucuna pruriens) from Nigeria Food Chem. 2000 421 427
    • (2000) Food Chem. , pp. 421-427
    • MacHuka, J.1
  • 29
    • 0348109377 scopus 로고    scopus 로고
    • Characterization of a proteinase inhibitor from Cajanus cajan (L.)
    • S.K. Haq, and R.H. Khan Characterization of a proteinase inhibitor from Cajanus cajan (L.) J. Protein Chem. 22 2003 543 554
    • (2003) J. Protein Chem. , vol.22 , pp. 543-554
    • Haq, S.K.1    Khan, R.H.2
  • 30
    • 0035735890 scopus 로고    scopus 로고
    • N- and O-linked oligosaccharides of allergenic glycoproteins
    • K. Fotisch, and S. Vieths N- and O-linked oligosaccharides of allergenic glycoproteins Glycoconj. J. 18 2001 373 390
    • (2001) Glycoconj. J. , vol.18 , pp. 373-390
    • Fotisch, K.1    Vieths, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.