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Volumn 106, Issue 1, 2008, Pages 1-8

Purification and characterization of a leucine aminopeptidase from the bovine filarial parasite Setaria cervi

Author keywords

ELISA; Filarial nematodes; Leucine aminopeptidase; Lymphatic filariasis; Metalloproteases; Setaria cervi; Western blotting

Indexed keywords

1,10 PHENANTHROLINE; AMASTATIN; ARYL ACYLAMIDASE; BESTATIN; BIOLOGICAL MARKER; COBALT; CYTOSOL AMINOPEPTIDASE; EDETIC ACID; GLUTAMINE; GLYCINE; LEUCINE; LEUCYL 2 NAPHTHYLAMIDE; MAGNESIUM ION; MANGANESE; PEPTIDE; PUROMYCIN; UNCLASSIFIED DRUG;

EID: 40849114447     PISSN: 0001706X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actatropica.2007.12.009     Document Type: Article
Times cited : (16)

References (53)
  • 1
    • 0031894438 scopus 로고    scopus 로고
    • Characterization and partial purification of a leucine aminopeptidase from Fasciola hepatica
    • Acosta D., Goni F., and Carmona C. Characterization and partial purification of a leucine aminopeptidase from Fasciola hepatica. J. Parasitol. 84 (1998) 1-7
    • (1998) J. Parasitol. , vol.84 , pp. 1-7
    • Acosta, D.1    Goni, F.2    Carmona, C.3
  • 3
    • 13944278892 scopus 로고    scopus 로고
    • RNAi-based discovery and validation of new drug targets in filarial nematodes
    • Behm C.A., Bendig M.M., McCarter J.P., and Sluder A.E. RNAi-based discovery and validation of new drug targets in filarial nematodes. Trends Parasitol. 21 (2005) 97-100
    • (2005) Trends Parasitol. , vol.21 , pp. 97-100
    • Behm, C.A.1    Bendig, M.M.2    McCarter, J.P.3    Sluder, A.E.4
  • 4
    • 21644465014 scopus 로고    scopus 로고
    • Detection and quantification of leucyl aminopeptidase after native electrophoresis using leucine-p-nitroanilide
    • Bozić N., and Vujcić Z. Detection and quantification of leucyl aminopeptidase after native electrophoresis using leucine-p-nitroanilide. Electrophoresis 26 (2005) 2476-2480
    • (2005) Electrophoresis , vol.26 , pp. 2476-2480
    • Bozić, N.1    Vujcić, Z.2
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford J. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, J.1
  • 6
    • 0242290371 scopus 로고    scopus 로고
    • The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction
    • Brooks D.R., Hooper N.M., and Isaac R.E. The Caenorhabditis elegans orthologue of mammalian puromycin-sensitive aminopeptidase has roles in embryogenesis and reproduction. J. Biol. Chem. 278 (2003) 42795-42801
    • (2003) J. Biol. Chem. , vol.278 , pp. 42795-42801
    • Brooks, D.R.1    Hooper, N.M.2    Isaac, R.E.3
  • 7
    • 0015501715 scopus 로고
    • Intermolecular cross-linking of monomeric proteins and cross-linking of oligomeric proteins as a probe of quaternary structure: application to leucine aminopeptidase (bovine lens)
    • Carpenter F.H., and Harrington K.T. Intermolecular cross-linking of monomeric proteins and cross-linking of oligomeric proteins as a probe of quaternary structure: application to leucine aminopeptidase (bovine lens). J. Biol. Chem. 247 (1972) 5580-5586
    • (1972) J. Biol. Chem. , vol.247 , pp. 5580-5586
    • Carpenter, F.H.1    Harrington, K.T.2
  • 8
    • 0015918807 scopus 로고
    • 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content
    • 2+ of the zinc metalloenzyme, amino acid composition, and sulfhydryl content. J. Biol. Chem. 248 (1973) 294-304
    • (1973) J. Biol. Chem. , vol.248 , pp. 294-304
    • Carpenter, F.H.1    Vahl, J.M.2
  • 9
    • 0034642182 scopus 로고    scopus 로고
    • Cloning, expression and characterization of human cytosolic aminopeptidase P: a single manganese (II)-dependent enzyme
    • Cottrell G.S., Hooper N.M., and Turner A.J. Cloning, expression and characterization of human cytosolic aminopeptidase P: a single manganese (II)-dependent enzyme. Biochemistry 39 (2000) 15121-15128
    • (2000) Biochemistry , vol.39 , pp. 15121-15128
    • Cottrell, G.S.1    Hooper, N.M.2    Turner, A.J.3
  • 10
    • 0014325813 scopus 로고
    • Moulting in a parasitic nematode Phocanema decipiens. IV: ecdysis and its control
    • Davey K.G., and Kan S.P. Moulting in a parasitic nematode Phocanema decipiens. IV: ecdysis and its control. Can. J. Zool. 46 (1968) 893-898
    • (1968) Can. J. Zool. , vol.46 , pp. 893-898
    • Davey, K.G.1    Kan, S.P.2
  • 11
    • 0033600583 scopus 로고    scopus 로고
    • The methionyl aminopeptidase from Escherichia coli can function as an iron (II) enzyme
    • D'Souza V.M., and Holz R.C. The methionyl aminopeptidase from Escherichia coli can function as an iron (II) enzyme. Biochemistry 38 (1999) 11079-11085
    • (1999) Biochemistry , vol.38 , pp. 11079-11085
    • D'Souza, V.M.1    Holz, R.C.2
  • 12
    • 0016806104 scopus 로고
    • Human liver alanine aminopeptidase. Inhibition by amino acids
    • Garner C.W., and Behal F.J. Human liver alanine aminopeptidase. Inhibition by amino acids. Biochemistry 14 (1975) 3208
    • (1975) Biochemistry , vol.14 , pp. 3208
    • Garner, C.W.1    Behal, F.J.2
  • 13
    • 0035451816 scopus 로고    scopus 로고
    • Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism
    • Gilboa R., Spungin-Bialik A., Wohlfahrt G., Schomburg D., Blumberg S., and Shoham G. Interactions of Streptomyces griseus aminopeptidase with amino acid reaction products and their implications toward a catalytic mechanism. Proteins Struct. Funct. Genet. 44 (2001) 490-504
    • (2001) Proteins Struct. Funct. Genet. , vol.44 , pp. 490-504
    • Gilboa, R.1    Spungin-Bialik, A.2    Wohlfahrt, G.3    Schomburg, D.4    Blumberg, S.5    Shoham, G.6
  • 14
    • 0036229654 scopus 로고    scopus 로고
    • Identification of residues critical for activity of the wound induced leucine aminopeptidase (LAP-A) of tomato
    • Gu Y.Q., and Walling L.L. Identification of residues critical for activity of the wound induced leucine aminopeptidase (LAP-A) of tomato. Eur. J. Biochem. 269 (2002) 1630-1640
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1630-1640
    • Gu, Y.Q.1    Walling, L.L.2
  • 15
    • 0000601032 scopus 로고    scopus 로고
    • A complex array of proteins related to the multimeric leucine aminopeptidase of tomato
    • Gu Y.-Q., Pautot V., Holzer F.M., and Walling L.L. A complex array of proteins related to the multimeric leucine aminopeptidase of tomato. Plant Physiol. 110 (1996) 1257-1266
    • (1996) Plant Physiol. , vol.110 , pp. 1257-1266
    • Gu, Y.-Q.1    Pautot, V.2    Holzer, F.M.3    Walling, L.L.4
  • 17
    • 0014599192 scopus 로고
    • Leucine aminopeptidase: a zinc metalloenzyme
    • Himmelhoch S. Leucine aminopeptidase: a zinc metalloenzyme. Arch. Biochem. Biophys. 134 (1969) 597-602
    • (1969) Arch. Biochem. Biophys. , vol.134 , pp. 597-602
    • Himmelhoch, S.1
  • 18
    • 0027289146 scopus 로고
    • Brugia pahangi: identification and characterization of an aminopeptidase associated with larval moulting
    • Hong X., Bouvier J., Wong M.M., Yamagata G.Y.L., and McKerrow J.H. Brugia pahangi: identification and characterization of an aminopeptidase associated with larval moulting. Exp. Parasitol. 76 (1993) 127-133
    • (1993) Exp. Parasitol. , vol.76 , pp. 127-133
    • Hong, X.1    Bouvier, J.2    Wong, M.M.3    Yamagata, G.Y.L.4    McKerrow, J.H.5
  • 19
    • 0033786019 scopus 로고    scopus 로고
    • Simple 1,2-amino alcohols as strain-specific antimalarial agents
    • Howarth J., and Lloyd D.G. Simple 1,2-amino alcohols as strain-specific antimalarial agents. J. Antimicrob. Chemother. 46 (2000) 625-627
    • (2000) J. Antimicrob. Chemother. , vol.46 , pp. 625-627
    • Howarth, J.1    Lloyd, D.G.2
  • 20
    • 0035815332 scopus 로고    scopus 로고
    • Functional analysis of leucine aminopeptidase in Caenorhabditis elegans
    • Joshua G.W.P. Functional analysis of leucine aminopeptidase in Caenorhabditis elegans. Mol. Biochem. Parasitol. 113 (2001) 223-232
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 223-232
    • Joshua, G.W.P.1
  • 21
    • 0023223711 scopus 로고
    • Identification of antigenic proteins of Setaria cervi by immunoblotting techniques
    • Kaushal N.A., Kaushal D.C., and Ghatak S. Identification of antigenic proteins of Setaria cervi by immunoblotting techniques. Immunol. Invest. 16 (1987) 139-149
    • (1987) Immunol. Invest. , vol.16 , pp. 139-149
    • Kaushal, N.A.1    Kaushal, D.C.2    Ghatak, S.3
  • 22
    • 0012295413 scopus 로고
    • Zur Bedeutung des Zinks in der Leucinaminopeptidase aus Rinderaugenlinsen
    • Kettman U., and Hanson H. Zur Bedeutung des Zinks in der Leucinaminopeptidase aus Rinderaugenlinsen. FEBS Lett. 10 (1970) 17-20
    • (1970) FEBS Lett. , vol.10 , pp. 17-20
    • Kettman, U.1    Hanson, H.2
  • 23
    • 0028045722 scopus 로고
    • Structure and mechanism of bovine lens leucine aminopeptidase
    • Kim H., and Lipscomb W.N. Structure and mechanism of bovine lens leucine aminopeptidase. Adv. Enzymol. Relat. Areas Mol. Biol. 68 (1994) 153-213
    • (1994) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.68 , pp. 153-213
    • Kim, H.1    Lipscomb, W.N.2
  • 24
    • 0027169053 scopus 로고
    • The effects of arphamenine-A, an inhibitor of aminopeptidases, on in vitro growth of Trypanosoma brucei
    • Knowles G. The effects of arphamenine-A, an inhibitor of aminopeptidases, on in vitro growth of Trypanosoma brucei. J. Antimicrob. Chemother. 32 (1993) 172-174
    • (1993) J. Antimicrob. Chemother. , vol.32 , pp. 172-174
    • Knowles, G.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0023869960 scopus 로고
    • Filarial antigen in circulating immune complexes from patients with Wuchereria bancrofti filariasis
    • Lunde M.L., Paranjape R., Lawley T.J., and Ottesen E.A. Filarial antigen in circulating immune complexes from patients with Wuchereria bancrofti filariasis. Am. J. Trop. Med. Hyg. 38 (1988) 366-371
    • (1988) Am. J. Trop. Med. Hyg. , vol.38 , pp. 366-371
    • Lunde, M.L.1    Paranjape, R.2    Lawley, T.J.3    Ottesen, E.A.4
  • 27
    • 0023480665 scopus 로고
    • Relationship between exsheathment and enzyme activity (alkaline phosphatase and leucine aminopeptidase) during ageing of Trichostrongylus colubriformis infective larvae
    • Malet S., and Lesage M.C. Relationship between exsheathment and enzyme activity (alkaline phosphatase and leucine aminopeptidase) during ageing of Trichostrongylus colubriformis infective larvae. Ann. Res. Vet. 18 (1987) 275-278
    • (1987) Ann. Res. Vet. , vol.18 , pp. 275-278
    • Malet, S.1    Lesage, M.C.2
  • 30
    • 0036973250 scopus 로고    scopus 로고
    • Lymphatic filariasis elimination: progress in global programme development
    • Molyneux D.H., and Zagaria N. Lymphatic filariasis elimination: progress in global programme development. Ann. Trop. Med. Parasitol. 96 (2002) S15-S40
    • (2002) Ann. Trop. Med. Parasitol. , vol.96
    • Molyneux, D.H.1    Zagaria, N.2
  • 31
    • 0037135520 scopus 로고    scopus 로고
    • Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species
    • Morty R.E., and Morehead J. Cloning and characterization of a leucyl aminopeptidase from three pathogenic Leishmania species. J. Biol. Chem. 277 (2002) 26057-26065
    • (2002) J. Biol. Chem. , vol.277 , pp. 26057-26065
    • Morty, R.E.1    Morehead, J.2
  • 32
    • 0031878901 scopus 로고    scopus 로고
    • Plasmodium chabaudi chabaudi and Plasmodium falciparum: inhibition of aminopeptidase and parasite growth by bestatin and nitrobestatin
    • Nankya-Kitaka M.F., Curley P.G., Gavigan C.S., Bell A., and Dalton J.P. Plasmodium chabaudi chabaudi and Plasmodium falciparum: inhibition of aminopeptidase and parasite growth by bestatin and nitrobestatin. Parasitol. Res. 84 (1998) 552-558
    • (1998) Parasitol. Res. , vol.84 , pp. 552-558
    • Nankya-Kitaka, M.F.1    Curley, P.G.2    Gavigan, C.S.3    Bell, A.4    Dalton, J.P.5
  • 33
    • 0004239251 scopus 로고    scopus 로고
    • Nutman T.B. (Ed), Imperial College Press, London
    • Nutman T.B. In: Nutman T.B. (Ed). Lymphatic Filariasis (2000), Imperial College Press, London
    • (2000) Lymphatic Filariasis
    • Nutman, T.B.1
  • 34
    • 0032733736 scopus 로고    scopus 로고
    • Rabbit kidney aminopeptidases: purification and some properties
    • Oliveira S.M., Freitas Jr. J.O., and Alves K.B. Rabbit kidney aminopeptidases: purification and some properties. Immunopharmacology 45 (1999) 215-221
    • (1999) Immunopharmacology , vol.45 , pp. 215-221
    • Oliveira, S.M.1    Freitas Jr., J.O.2    Alves, K.B.3
  • 35
    • 0033034097 scopus 로고    scopus 로고
    • Vaccination with cathepsin l proteinases and with leucine aminopeptidase induces high levels of protection against fasciolosis in sheep
    • Piacenza L., Acosta D., Basmadjian I., Dalton J.P., and Carmona C. Vaccination with cathepsin l proteinases and with leucine aminopeptidase induces high levels of protection against fasciolosis in sheep. Infect. Immun. 67 (1999) 1954-1961
    • (1999) Infect. Immun. , vol.67 , pp. 1954-1961
    • Piacenza, L.1    Acosta, D.2    Basmadjian, I.3    Dalton, J.P.4    Carmona, C.5
  • 36
    • 33745475040 scopus 로고    scopus 로고
    • Tissue localization of collagenase and leucine aminopeptidase of a bovine filarial parasite Setaria cervi
    • Pokharel D.R., Rai R., Kumar P., Chaturvedi C.M., and Rathaur S. Tissue localization of collagenase and leucine aminopeptidase of a bovine filarial parasite Setaria cervi. Filaria J. 5 (2006) 7
    • (2006) Filaria J. , vol.5 , pp. 7
    • Pokharel, D.R.1    Rai, R.2    Kumar, P.3    Chaturvedi, C.M.4    Rathaur, S.5
  • 37
    • 0023493918 scopus 로고
    • Secretory acetylcholinesterase from Brugia malayi adult and microfilarial parasites
    • Rathaur S., Robertson B.D., Selkirk M.E., and Maizels R.M. Secretory acetylcholinesterase from Brugia malayi adult and microfilarial parasites. Mol. Biochem. Parasitol. 26 (1987) 257-265
    • (1987) Mol. Biochem. Parasitol. , vol.26 , pp. 257-265
    • Rathaur, S.1    Robertson, B.D.2    Selkirk, M.E.3    Maizels, R.M.4
  • 38
    • 0032211405 scopus 로고    scopus 로고
    • Purification and characterisation of a secreted aminopeptidase from adult Ascaris suum
    • Rhoads M.L., and Fetterer R.H. Purification and characterisation of a secreted aminopeptidase from adult Ascaris suum. Int. J. Parasitol. 28 (1998) 1681-1690
    • (1998) Int. J. Parasitol. , vol.28 , pp. 1681-1690
    • Rhoads, M.L.1    Fetterer, R.H.2
  • 39
    • 0026914848 scopus 로고
    • Dirofilaria immitis: proteases produced by third- and fourth stage larvae
    • Richer J.K., Sakanari J.A., Frank G.R., and Grieve R.B. Dirofilaria immitis: proteases produced by third- and fourth stage larvae. Exp. Parasitol. 75 (1992) 213-222
    • (1992) Exp. Parasitol. , vol.75 , pp. 213-222
    • Richer, J.K.1    Sakanari, J.A.2    Frank, G.R.3    Grieve, R.B.4
  • 40
    • 0017936881 scopus 로고
    • Leucine aminopeptidase in exsheathing fluid of North American and Australian Haemonchus contortus
    • Rogers W.P., and Brooks F. Leucine aminopeptidase in exsheathing fluid of North American and Australian Haemonchus contortus. Int. J. Parasitol. 8 (1978) 55-58
    • (1978) Int. J. Parasitol. , vol.8 , pp. 55-58
    • Rogers, W.P.1    Brooks, F.2
  • 41
    • 0344927947 scopus 로고
    • The role of leucine aminopeptidase in the molting of nematode parasites
    • Rogers W.P. The role of leucine aminopeptidase in the molting of nematode parasites. Comp. Biochem. Physiol. 14 (1965) 311-316
    • (1965) Comp. Biochem. Physiol. , vol.14 , pp. 311-316
    • Rogers, W.P.1
  • 42
    • 0020391316 scopus 로고
    • Enzymes in the exsheathing fluid of nematodes and their biological significance
    • Rogers W.P. Enzymes in the exsheathing fluid of nematodes and their biological significance. Int. J. Parasitol. 12 (1982) 495-502
    • (1982) Int. J. Parasitol. , vol.12 , pp. 495-502
    • Rogers, W.P.1
  • 44
    • 0031890110 scopus 로고    scopus 로고
    • Secretory acetylcholinesterase of Setaria cervi microfilariae and its antigenic cross-reactivity with Wuchereria bancrofti
    • Sharma S., Mishra S., and Rathaur S. Secretory acetylcholinesterase of Setaria cervi microfilariae and its antigenic cross-reactivity with Wuchereria bancrofti. Trop. Med. Int. Health 3 (1998) 46-51
    • (1998) Trop. Med. Int. Health , vol.3 , pp. 46-51
    • Sharma, S.1    Mishra, S.2    Rathaur, S.3
  • 45
    • 18944386580 scopus 로고    scopus 로고
    • Identification and characterization of a selenium-dependent glutathione peroxidase in Setaria cervi
    • Singh A., and Rathaur S. Identification and characterization of a selenium-dependent glutathione peroxidase in Setaria cervi. Biochem. Biophys. Res. Commun. 331 (2006) 1069-1074
    • (2006) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1069-1074
    • Singh, A.1    Rathaur, S.2
  • 46
    • 0001624667 scopus 로고
    • Leucine aminopeptidase V. Activation, specificity, and mechanism of action
    • Smith E.L., and Spackman D.H. Leucine aminopeptidase V. Activation, specificity, and mechanism of action. J. Biol. Chem. 212 (1955) 271-299
    • (1955) J. Biol. Chem. , vol.212 , pp. 271-299
    • Smith, E.L.1    Spackman, D.H.2
  • 47
    • 0013672232 scopus 로고    scopus 로고
    • Clan MF containing co-catalytic leucyl aminopeptidases
    • Barrett A.J., Rawlings N., and Woessner J.F. (Eds), Academic Press, London
    • Strater N., and Lipscomb W.N. Clan MF containing co-catalytic leucyl aminopeptidases. In: Barrett A.J., Rawlings N., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes (1998), Academic Press, London 1382-1389
    • (1998) Handbook of Proteolytic Enzymes , pp. 1382-1389
    • Strater, N.1    Lipscomb, W.N.2
  • 48
    • 0027479013 scopus 로고
    • Aminopeptidases: structure and function
    • Taylor A. Aminopeptidases: structure and function. FASEB J. 7 (1993) 290-298
    • (1993) FASEB J. , vol.7 , pp. 290-298
    • Taylor, A.1
  • 49
    • 0017236348 scopus 로고
    • Bestatin, an inhibitor of aminopeptidase B, produced by actinomyces
    • Umezawa H., Aoyagi T., Suda H., Hamada M., and Takeuchi T. Bestatin, an inhibitor of aminopeptidase B, produced by actinomyces. J. Antibiot. 29 (1976) 97-99
    • (1976) J. Antibiot. , vol.29 , pp. 97-99
    • Umezawa, H.1    Aoyagi, T.2    Suda, H.3    Hamada, M.4    Takeuchi, T.5
  • 50
    • 0014962699 scopus 로고
    • Purification and properties of an aminopeptidase from Escherichia coli
    • Vogt V. Purification and properties of an aminopeptidase from Escherichia coli. J. Biol. Chem. 245 (1970) 4760-4769
    • (1970) J. Biol. Chem. , vol.245 , pp. 4760-4769
    • Vogt, V.1
  • 51
    • 0031703555 scopus 로고    scopus 로고
    • 2+ as a cofactor: a case of mistaken identity?
    • 2+ as a cofactor: a case of mistaken identity?. Protein Sci. 7 (1998) 2684-2687
    • (1998) Protein Sci. , vol.7 , pp. 2684-2687
    • Walker, K.W.1    Bradshaw, R.A.2
  • 53
    • 0022974175 scopus 로고
    • Leucine aminopeptidase and hatching of Schistosoma mansoni eggs
    • Xu Y.Z., and Dresden M.H. Leucine aminopeptidase and hatching of Schistosoma mansoni eggs. J. Parasitol. 72 (1986) 507-511
    • (1986) J. Parasitol. , vol.72 , pp. 507-511
    • Xu, Y.Z.1    Dresden, M.H.2


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