메뉴 건너뛰기




Volumn 16, Issue 12, 2009, Pages 1526-1532

Two kunitz-type inhibitors with activity against trypsin and papain from Pithecellobium dumosum seeds: Purification, characterization, and activity towards pest insect digestive enzyme

Author keywords

Kunitz inhibitor; Leguminosae; Pest proteases; Pithecellobium dumosum

Indexed keywords

BROMELAIN; CHYMOTRYPSIN; KUNITZ TYPE PROTEASE INHIBITOR, PLANT; KUNITZ-TYPE PROTEASE INHIBITOR, PLANT; PANCREATIC ELASTASE; PAPAIN; PDKI 3.1 PROTEIN, PITHECELLOBIUM DUMOSUM; PDKI 3.2 PROTEIN, PITHECELLOBIUM DUMOSUM; PDKI-3.1 PROTEIN, PITHECELLOBIUM DUMOSUM; PDKI-3.2 PROTEIN, PITHECELLOBIUM DUMOSUM; PEPTIDE; TRYPSIN; VEGETABLE PROTEIN;

EID: 73449118609     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789839403     Document Type: Article
Times cited : (15)

References (51)
  • 1
    • 0018873523 scopus 로고
    • Protein inhibitors of proteinases
    • Laskowski, M.; Kato, I. Protein inhibitors of proteinases. Annu. Rev. Biochem., 1980, 49, 593-626.
    • (1980) Annu. Rev. Biochem , vol.49 , pp. 593-626
    • Laskowski, M.1    Kato, I.2
  • 2
    • 15444362114 scopus 로고    scopus 로고
    • Proteinases and their inhibitors in plants: Role in normal growth and in response to various stress conditions M
    • Brzin, J.; Kidric, M. Proteinases and their inhibitors in plants: role in normal growth and in response to various stress conditions M. Biotechnol. Genet. Eng. Rev., 1996, 13, 421-467.
    • (1996) Biotechnol. Genet. Eng. Rev , vol.13 , pp. 421-467
    • Brzin, J.1    Kidric, M.2
  • 3
    • 77956761508 scopus 로고    scopus 로고
    • Plant proteins that confer resistance to pests and pathogens, Advances in Botanical Research Incorporating Advances in Plant
    • Shewry, P. R.; Lucas, J. A. Plant proteins that confer resistance to pests and pathogens, Advances in Botanical Research Incorporating Advances in Plant. Adv. Bot. Res., 1997, 26, 135-192.
    • (1997) Adv. Bot. Res , vol.26 , pp. 135-192
    • Shewry, P.R.1    Lucas, J.A.2
  • 4
    • 0008500304 scopus 로고
    • The biological roles of serine and cysteine proteinase inhibitors in plants
    • Xavier-Filho, J. The biological roles of serine and cysteine proteinase inhibitors in plants. R. Bras. Fisiol. Veg., 1992, 4, 1-6.
    • (1992) R. Bras. Fisiol. Veg , vol.4 , pp. 1-6
    • Xavier-Filho, J.1
  • 5
    • 0000180578 scopus 로고
    • Seed storage proteins: The enzyme inhibitor in Methods in Plant Biochemistry
    • Ryan, C. A. Seed storage proteins: The enzyme inhibitor in Methods in Plant Biochemistry Ann. Rev. Phytol., 1991, 28, 425-449.
    • (1991) Ann. Rev. Phytol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 6
    • 0033101490 scopus 로고    scopus 로고
    • The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants
    • Solomon, M.; Belenghi, B.; Delledonne, M.; Menachem, E.; Levine, A. The involvement of cysteine proteases and protease inhibitor genes in the regulation of programmed cell death in plants. Plant Cell, 1999, 11, 431-443.
    • (1999) Plant Cell , vol.11 , pp. 431-443
    • Solomon, M.1    Belenghi, B.2    Delledonne, M.3    Menachem, E.4    Levine, A.5
  • 7
    • 0034341051 scopus 로고    scopus 로고
    • Franco, O. L.; Melo, F. R. Osmoprotectants, a plant strategy in response to osmotic stress. J. Plant. Physiol., 2000, 47, 137-144.
    • Franco, O. L.; Melo, F. R. Osmoprotectants, a plant strategy in response to osmotic stress. J. Plant. Physiol., 2000, 47, 137-144.
  • 8
    • 0031887585 scopus 로고    scopus 로고
    • Identifying proteins with insecticidal activity: Use of encoding genes to produce insectresistant transgenic crops
    • Gatehouse, A. M. R.; Gatehouse, J. A. Identifying proteins with insecticidal activity: use of encoding genes to produce insectresistant transgenic crops. Pestic. Sci., 1998, 52, 165-175.
    • (1998) Pestic. Sci , vol.52 , pp. 165-175
    • Gatehouse, A.M.R.1    Gatehouse, J.A.2
  • 9
    • 0033016160 scopus 로고    scopus 로고
    • Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo
    • Gatehouse, A. M. R.; Norton, E.; Davison, G. M.; Babbe, S. M.; Newell, C. A.; Gatehouse, J. A. Digestive proteolytic activity in larvae of tomato moth, Lacanobia oleracea; effects of plant protease inhibitors in vitro and in vivo. J. Insect Physiol., 1999, 45, 545-558.
    • (1999) J. Insect Physiol , vol.45 , pp. 545-558
    • Gatehouse, A.M.R.1    Norton, E.2    Davison, G.M.3    Babbe, S.M.4    Newell, C.A.5    Gatehouse, J.A.6
  • 10
    • 0001144526 scopus 로고
    • Seed storage proteins: The enzyme inhibitors
    • Richardson, M. Seed storage proteins: the enzyme inhibitors Methods in Plant. Biochemistry., 1991, 5, 259-305.
    • (1991) Methods in Plant. Biochemistry , vol.5 , pp. 259-305
    • Richardson, M.1
  • 11
    • 20744458540 scopus 로고    scopus 로고
    • Araujo, C. L.; Bezerra, I. W. L.; Oliveira, A. S.; Moura, F. T.; Macedo, L. L. P.; Gomes, C. E. M.; Barbosa, A. E. A. D.; Macedo, F. P.; Souza, T. M. S.; Franco, O. L.; Bloch-J, C.; Sales, M. P. In vivo bioinsecticidal activity toward Ceratitis capitata (Fruit fly) and Callosobruchus maculatus (Cowpea weevil) and in vitro bioinsecticidal activity toward different orders of insect pests of a trypsin inhibitor purified from tamarind tree (Tamarindus indica) seeds. J. Agric. Food Chem., 2005, 53, 4381-4387.
    • Araujo, C. L.; Bezerra, I. W. L.; Oliveira, A. S.; Moura, F. T.; Macedo, L. L. P.; Gomes, C. E. M.; Barbosa, A. E. A. D.; Macedo, F. P.; Souza, T. M. S.; Franco, O. L.; Bloch-J, C.; Sales, M. P. In vivo bioinsecticidal activity toward Ceratitis capitata (Fruit fly) and Callosobruchus maculatus (Cowpea weevil) and in vitro bioinsecticidal activity toward different orders of insect pests of a trypsin inhibitor purified from tamarind tree (Tamarindus indica) seeds. J. Agric. Food Chem., 2005, 53, 4381-4387.
  • 15
    • 30344443076 scopus 로고    scopus 로고
    • A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: Purification, characterization, and kinetic properties
    • Bhattacharyya, A.; Mazumdar, S.; Leighton, S. M.; Babu, C. R. A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: Purification, characterization, and kinetic properties. Phytochemistry, 2006, 67 232-241.
    • (2006) Phytochemistry , vol.67 , pp. 232-241
    • Bhattacharyya, A.1    Mazumdar, S.2    Leighton, S.M.3    Babu, C.R.4
  • 16
    • 34047194820 scopus 로고    scopus 로고
    • Characterization of a Kunitz trypsin inhibitor with a single disulfide bridge from seeds of Inga laurina (SW.) Willd
    • Macedo, M. L. R.; Garcia, V. A.; Freire, M. G.; Richardson, M. Characterization of a Kunitz trypsin inhibitor with a single disulfide bridge from seeds of Inga laurina (SW.) Willd.. Phytochemistry, 2007, 68, 1104-1111.
    • (2007) Phytochemistry , vol.68 , pp. 1104-1111
    • Macedo, M.L.R.1    Garcia, V.A.2    Freire, M.G.3    Richardson, M.4
  • 17
    • 0034615564 scopus 로고    scopus 로고
    • Structural basis of the endoproteinase-protein inhibitor interaction
    • Bode, W.; Huber, R. Structural basis of the endoproteinase-protein inhibitor interaction. Biochim. Biophys. Acta, 2000, 1477, 241-252.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 241-252
    • Bode, W.1    Huber, R.2
  • 19
    • 0242500472 scopus 로고    scopus 로고
    • A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera : Pyralidae)
    • Macedo, M. L. R.; Freire, M. D. M.; Cabrini, E. C.; Toyama, M. H.; Novello, J. C.; Marangoni, S. A trypsin inhibitor from Peltophorum dubium seeds active against pest proteases and its effect on the survival of Anagasta kuehniella (Lepidoptera : Pyralidae). Biochim. Biophys. Acta, 2003, 1621, 170-182.
    • (2003) Biochim. Biophys. Acta , vol.1621 , pp. 170-182
    • Macedo, M.L.R.1    Freire, M.D.M.2    Cabrini, E.C.3    Toyama, M.H.4    Novello, J.C.5    Marangoni, S.6
  • 20
    • 2342519504 scopus 로고    scopus 로고
    • A Kunitz-type inhibitor of coleopteran proteases, isolated from Adenanthera davonina L. seeds and its effect on Callosobruchus maculates
    • Macedo, M. L. R.; De Sa, C. M.; Freire, M. D. M.; Parra, J. R. P. A Kunitz-type inhibitor of coleopteran proteases, isolated from Adenanthera davonina L. seeds and its effect on Callosobruchus maculates. J. Agric. Food. Chem., 2004, 52, 2533-2540.
    • (2004) J. Agric. Food. Chem , vol.52 , pp. 2533-2540
    • Macedo, M.L.R.1    De Sa, C.M.2    Freire, M.D.M.3    Parra, J.R.P.4
  • 21
    • 34247358675 scopus 로고    scopus 로고
    • Bioinsecticidal activity of Archidendron ellipticum trypsin inhibitor on growth and serine digestive enzymes during larval development of Spodoptera litura
    • Bhattacharyya, A.; Rai, A. S.; Babu, C. R. Bioinsecticidal activity of Archidendron ellipticum trypsin inhibitor on growth and serine digestive enzymes during larval development of Spodoptera litura. Plant Physiol. Biochem., 2007, 45, 169-177.
    • (2007) Plant Physiol. Biochem , vol.45 , pp. 169-177
    • Bhattacharyya, A.1    Rai, A.S.2    Babu, C.R.3
  • 24
    • 0017184389 scopus 로고
    • Rapid and Sensitive Method for Quantitation of Microgram Quantities of Protein Utilizing Principle of Protein-Dye Binding
    • Bradford, M. M. Rapid and Sensitive Method for Quantitation of Microgram Quantities of Protein Utilizing Principle of Protein-Dye Binding. Anal. Biochem., 1976, 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0013924977 scopus 로고
    • The action of chymotrypsin on two new chromogenic substrates
    • Erlanger, B. F.; Edel, F.; Cooper, A. G. The action of chymotrypsin on two new chromogenic substrates. Arch. Biochem. Biophys., 1966, 115, 206-278.
    • (1966) Arch. Biochem. Biophys , vol.115 , pp. 206-278
    • Erlanger, B.F.1    Edel, F.2    Cooper, A.G.3
  • 26
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng, Y.; Prusoff, W. H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol., 1973, 22, 3099-3108.
    • (1973) Biochem. Pharmacol , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 27
    • 0030220996 scopus 로고    scopus 로고
    • Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog
    • Zhao, Y.; Botella, M. A.; Subramanian, L.; Niu, X. M.; Nielsen, S. S.; Bressan, R. A.; Hasegawa, P. M. Two wound-inducible soybean cysteine proteinase inhibitors have greater insect digestive proteinase inhibitory activities than a constitutive homolog. Plant Physiol., 1996, 111, 1299-1306.
    • (1996) Plant Physiol , vol.111 , pp. 1299-1306
    • Zhao, Y.1    Botella, M.A.2    Subramanian, L.3    Niu, X.M.4    Nielsen, S.S.5    Bressan, R.A.6    Hasegawa, P.M.7
  • 28
    • 0000736550 scopus 로고    scopus 로고
    • Xavier-Filho, J.; Campos, F. A. P.; Ary, M. B.; Silva, C. P.; Carvalho, M. M. M.; Macedo, M. L. R.; Lemos, F. J. A.; Poor correlation between the levels of proteinase inhibitors found in seeds of different cultivars of cowpea (Vigna unguiculata) and resistance/susceptibility to predation by Callosobruchus maculates. Grant, G. J. Agric. Food Chem., 1989, 37, 1139-1143.
    • Xavier-Filho, J.; Campos, F. A. P.; Ary, M. B.; Silva, C. P.; Carvalho, M. M. M.; Macedo, M. L. R.; Lemos, F. J. A.; Poor correlation between the levels of proteinase inhibitors found in seeds of different cultivars of cowpea (Vigna unguiculata) and resistance/susceptibility to predation by Callosobruchus maculates. Grant, G. J. Agric. Food Chem., 1989, 37, 1139-1143.
  • 29
    • 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, 680-690.
    • (1970) Nature , vol.227 , pp. 680-690
    • Laemmli, U.K.1
  • 30
    • 84988074679 scopus 로고
    • Improved silver staining of plantproteins, RNA and DNA in polyacrylamide gels
    • Bloom, H.; Beier, H.; Gross, H. J. Improved silver staining of plantproteins, RNA and DNA in polyacrylamide gels. Electrophoresis, 1987, 8, 93-99.
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Bloom, H.1    Beier, H.2    Gross, H.J.3
  • 31
    • 0001961243 scopus 로고
    • Purification and Partial Characterization of Trypsin-Inhibitors from Seeds of Clitoria ternatea
    • Macedo, M. L. R.; Xavier-Filho, J. Purification and Partial Characterization of Trypsin-Inhibitors from Seeds of Clitoria ternatea. J. Sci. Food Agric., 1992, 58, 55-58.
    • (1992) J. Sci. Food Agric , vol.58 , pp. 55-58
    • Macedo, M.L.R.1    Xavier-Filho, J.2
  • 34
    • 45949130041 scopus 로고
    • The Amino-Acid-Sequence and Reactive (Inhibitory) Site of the Major Trypsin Isoinhibitor (De5) Isolated from Seeds of the Brazilian Carolina Tree (Adenanthera-Pavonina L)
    • Richardson, M.; Campos, F. A. P.; Xavier-Filho, J.; Macedo, M. L. R.; Maia, G. M. C.; Yarwood, A. The Amino-Acid-Sequence and Reactive (Inhibitory) Site of the Major Trypsin Isoinhibitor (De5) Isolated from Seeds of the Brazilian Carolina Tree (Adenanthera-Pavonina L). Biochim. Biophys. Acta, 1986, 872, 134-140.
    • (1986) Biochim. Biophys. Acta , vol.872 , pp. 134-140
    • Richardson, M.1    Campos, F.A.P.2    Xavier-Filho, J.3    Macedo, M.L.R.4    Maia, G.M.C.5    Yarwood, A.6
  • 35
    • 0027414116 scopus 로고
    • The complete amino acid sequence of a Kunitz family trypsin inhibitor from seeds of Acacia confusa
    • Wu, H. C.; Lin, J. Y. The complete amino acid sequence of a Kunitz family trypsin inhibitor from seeds of Acacia confusa. J. Biochem., 1993, 113, 258-263.
    • (1993) J. Biochem , vol.113 , pp. 258-263
    • Wu, H.C.1    Lin, J.Y.2
  • 36
    • 0024991650 scopus 로고
    • Regulation of coagulation by a multivalent Kunitz-type inhibitor
    • Broze, G. J.; Girard, T. J. Regulation of coagulation by a multivalent Kunitz-type inhibitor. J. Biochem., 1990, 29, 7539-7546.
    • (1990) J. Biochem , vol.29 , pp. 7539-7546
    • Broze, G.J.1    Girard, T.J.2
  • 37
    • 52849091248 scopus 로고    scopus 로고
    • Effects of denaturing and stabilizing agents on the inhibitory activity and conformational stability of Schizolobium parahyba chymotrypsin inhibitor
    • Souza, E. M. T.; Teles, R. C. L.; Siqueira, E. M. D.; Freitas, S. M. Effects of denaturing and stabilizing agents on the inhibitory activity and conformational stability of Schizolobium parahyba chymotrypsin inhibitor. J. Protein Chem., 2000, 19, 507-513.
    • (2000) J. Protein Chem , vol.19 , pp. 507-513
    • Souza, E.M.T.1    Teles, R.C.L.2    Siqueira, E.M.D.3    Freitas, S.M.4
  • 38
    • 16544377766 scopus 로고    scopus 로고
    • Trypsin inhibitor from Poecilanthe parviflora seeds: Purification, characterization, and activity against pest proteases
    • Garcia, V. A.; Freire, M. G.; Novello, J. C.; Marangoni, S.; Macedo, M. L. Trypsin inhibitor from Poecilanthe parviflora seeds: Purification, characterization, and activity against pest proteases. Protein J., 2004, 23, 343-350.
    • (2004) Protein J , vol.23 , pp. 343-350
    • Garcia, V.A.1    Freire, M.G.2    Novello, J.C.3    Marangoni, S.4    Macedo, M.L.5
  • 40
    • 0019555769 scopus 로고
    • Acacia Proteinase-Inhibitors - Purification and Properties of the Trypsin-Inhibitors from Acacia-Elata Seed
    • Kortt, A. A.; Jermyn, M. A. Acacia Proteinase-Inhibitors - Purification and Properties of the Trypsin-Inhibitors from Acacia-Elata Seed. Eur. J. Biochem., 1981, 115, 551-557.
    • (1981) Eur. J. Biochem , vol.115 , pp. 551-557
    • Kortt, A.A.1    Jermyn, M.A.2
  • 41
    • 0029310522 scopus 로고
    • Purification and partial characterization of a Schizolobium parahyba chymotrypsin inhibitor
    • Souza, E. M. T.; Mizuta, K.; Sampaio, M. U.; Sampaio, C. A. M. Purification and partial characterization of a Schizolobium parahyba chymotrypsin inhibitor. Phytochemistry, 1995, 39, 521-525.
    • (1995) Phytochemistry , vol.39 , pp. 521-525
    • Souza, E.M.T.1    Mizuta, K.2    Sampaio, M.U.3    Sampaio, C.A.M.4
  • 42
    • 0033372407 scopus 로고    scopus 로고
    • Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds
    • Pando, L. A.; Di Ciero, L.; Novello, J. C.; Oliveira, B.; Weder, J. K. P.; Marangoni, S. Isolation and characterization of a new trypsin inhibitor from Crotalaria paulina seeds. Iubmb Life, 1999, 48, 519-523.
    • (1999) Iubmb Life , vol.48 , pp. 519-523
    • Pando, L.A.1    Di Ciero, L.2    Novello, J.C.3    Oliveira, B.4    Weder, J.K.P.5    Marangoni, S.6
  • 45
    • 0029977174 scopus 로고    scopus 로고
    • Midgut proteinases in three divergent species of Coleoptera
    • Terra, W. R.; Cristofoletti, P. T. Midgut proteinases in three divergent species of Coleoptera. Comp. Biochem. Physiol., 1996, 113, 725-730.
    • (1996) Comp. Biochem. Physiol , vol.113 , pp. 725-730
    • Terra, W.R.1    Cristofoletti, P.T.2
  • 46
    • 33745685458 scopus 로고    scopus 로고
    • Digestive enzymes during development of Ceratitis capitata (Diptera: Tephritidae) and effects of SBTI on its digestive serine proteinase targets
    • Silva, F. C. B. L.; Alcazar, A.; Macedo, L. L. P.; Oliveira, A. S.; Macedo, F. P.; Abreu, L. R. D.; Santos, E. A.; Sales, M. P. Digestive enzymes during development of Ceratitis capitata (Diptera: Tephritidae) and effects of SBTI on its digestive serine proteinase targets. Insect Biochem. Mol. Biol., 2006, 36, 561-569.
    • (2006) Insect Biochem. Mol. Biol , vol.36 , pp. 561-569
    • Silva, F.C.B.L.1    Alcazar, A.2    Macedo, L.L.P.3    Oliveira, A.S.4    Macedo, F.P.5    Abreu, L.R.D.6    Santos, E.A.7    Sales, M.P.8
  • 48
    • 0000128089 scopus 로고
    • Diversity in digestive proteinase activity among insects
    • Wolfson, J. L.; Murdock, L. L. Diversity in digestive proteinase activity among insects. J. Chem. Ecol., 1990, 16, 1089-1102.
    • (1990) J. Chem. Ecol , vol.16 , pp. 1089-1102
    • Wolfson, J.L.1    Murdock, L.L.2
  • 49
    • 0035070334 scopus 로고    scopus 로고
    • Biochemical characterization and N-terminal sequences of two new trypsin inhibitors from Copaifera langsdorffii seeds
    • Silva, J. A.; Macedo, M. L. R.; Novello, J. C.; Marangoni, S. Biochemical characterization and N-terminal sequences of two new trypsin inhibitors from Copaifera langsdorffii seeds. J. Protein Chem., 2001, 20, 1-7.
    • (2001) J. Protein Chem , vol.20 , pp. 1-7
    • Silva, J.A.1    Macedo, M.L.R.2    Novello, J.C.3    Marangoni, S.4
  • 50
    • 27944443661 scopus 로고    scopus 로고
    • Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects
    • Fan, S. G.; Wu, G. H. Characteristics of plant proteinase inhibitors and their applications in combating phytophagous insects. Bot. Bull. Acad. Sinica, 2005, 46, 273-292.
    • (2005) Bot. Bull. Acad. Sinica , vol.46 , pp. 273-292
    • Fan, S.G.1    Wu, G.H.2
  • 51
    • 34347386663 scopus 로고    scopus 로고
    • Plant protease inhibitors in control of phytophagous insects
    • Lawrence, P. K.; Koundal, K. R. Plant protease inhibitors in control of phytophagous insects. Electron. J. Biotechnol., 2002, 5, 93-109.
    • (2002) Electron. J. Biotechnol , vol.5 , pp. 93-109
    • Lawrence, P.K.1    Koundal, K.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.