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Volumn 234, Issue 4, 2011, Pages 723-735

WCI, a novel wheat chymotrypsin inhibitor: Purification, primary structure, inhibitory properties and heterologous expression

Author keywords

Cereal trypsin amylase inhibitor family; Phytophagous insect proteinases; Sequence analysis; Serine protease inhibitor; Triticum

Indexed keywords

CHYMOTRYPSIN; COMPLEMENTARY DNA; MESSENGER RNA; PLANT RNA; PROTEINASE INHIBITOR; VEGETABLE PROTEIN;

EID: 80955178854     PISSN: 00320935     EISSN: 14322048     Source Type: Journal    
DOI: 10.1007/s00425-011-1437-5     Document Type: Article
Times cited : (10)

References (37)
  • 1
    • 0038398775 scopus 로고    scopus 로고
    • Transgenic expression of trypsin inhibitor CMe from barley in indica and japonica rice, confers resistance to the rice weevil Sitophilus oryzae
    • Alfonso-Rubi J, Ortego F, Castanera P, Carbonero P, Diaz I (2003) Transgenic expression of trypsin inhibitor CMe from barley in indica and japonica rice, confers resistance to the rice weevil Sitophilus oryzae. Transgenic Res 12: 23-31.
    • (2003) Transgenic Res , vol.12 , pp. 23-31
    • Alfonso-Rubi, J.1    Ortego, F.2    Castanera, P.3    Carbonero, P.4    Diaz, I.5
  • 2
    • 46149127835 scopus 로고
    • Evolutionary implications of sequential homologies among members of the trypsin/α-amylase inhibitor family (CM proteins) in wheat and barley
    • Barber D, Sàncez-Monge R, Garcia-Olmedo F, Salcedo G, Mendez E (1986) Evolutionary implications of sequential homologies among members of the trypsin/α-amylase inhibitor family (CM proteins) in wheat and barley. Biochim Biophys Acta 873: 147-151.
    • (1986) Biochim Biophys Acta , vol.873 , pp. 147-151
    • Barber, D.1    Sàncez-Monge, R.2    Garcia-Olmedo, F.3    Salcedo, G.4    Mendez, E.5
  • 3
    • 0032480808 scopus 로고    scopus 로고
    • Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1.95 Å resolution
    • Behnke CA, Yee VC, Trong IL, Pedersen LC, Stenkamp RE, Kim SS, Reeck GR, Teller DC (1998) Structural determinants of the bifunctional corn Hageman factor inhibitor: X-ray crystal structure at 1. 95 Å resolution. Biochemistry 37: 15277-15288.
    • (1998) Biochemistry , vol.37 , pp. 15277-15288
    • Behnke, C.A.1    Yee, V.C.2    Trong, I.L.3    Pedersen, L.C.4    Stenkamp, R.E.5    Kim, S.S.6    Reeck, G.R.7    Teller, D.C.8
  • 5
    • 0026530977 scopus 로고
    • Natural protein proteinase inhibitors and their interaction with proteinases
    • Bode W, Huber R (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur J Biochem 204: 433-451.
    • (1992) Eur J Biochem , vol.204 , pp. 433-451
    • Bode, W.1    Huber, R.2
  • 6
    • 0012549412 scopus 로고
    • Trypsin inhibitor from wheat endosperm: purification and characterization
    • Boisen S, Djurtoft R (1981) Trypsin inhibitor from wheat endosperm: purification and characterization. Cereal Chem 58: 460-463.
    • (1981) Cereal Chem , vol.58 , pp. 460-463
    • Boisen, S.1    Djurtoft, R.2
  • 7
    • 27144500597 scopus 로고
    • Further identification of bean trypsin inhibiting factors
    • Bowman DE (1948) Further identification of bean trypsin inhibiting factors. Arch Biochem Biophys 16: 109-113.
    • (1948) Arch Biochem Biophys , vol.16 , pp. 109-113
    • Bowman, D.E.1
  • 8
    • 0019021452 scopus 로고
    • Interaction of wheat monomeric and dimeric protein inhibitors with alpha-amylase from yellow mealworm (Tenebrio molitor L. larva)
    • Buonocore V, Gramenzi F, Pace W, Petrucci T, Poerio E, Silano V (1980) Interaction of wheat monomeric and dimeric protein inhibitors with alpha-amylase from yellow mealworm (Tenebrio molitor L. larva). Biochem J 187: 637-645.
    • (1980) Biochem J , vol.187 , pp. 637-645
    • Buonocore, V.1    Gramenzi, F.2    Pace, W.3    Petrucci, T.4    Poerio, E.5    Silano, V.6
  • 9
    • 0016700753 scopus 로고
    • Tight-binding inhibitors-I. Kinetic behavior
    • Cha S (1975) Tight-binding inhibitors-I. Kinetic behavior. Biochem Pharmacol 24: 2177-2185.
    • (1975) Biochem Pharmacol , vol.24 , pp. 2177-2185
    • Cha, S.1
  • 11
    • 25144446868 scopus 로고    scopus 로고
    • cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests
    • Di Gennaro S, Ficca AG, Panichi D, Poerio E (2005) cDNA cloning and heterologous expression of a wheat proteinase inhibitor of subtilisin and chymotrypsin (WSCI) that interferes with digestive enzymes of insect pests. Biol Chem 386: 383-389.
    • (2005) Biol Chem , vol.386 , pp. 383-389
    • Di Gennaro, S.1    Ficca, A.G.2    Panichi, D.3    Poerio, E.4
  • 12
    • 0035137983 scopus 로고    scopus 로고
    • Reliable sequence determination of ribosome- inactivating proteins by combining electrospray mass spectrometry and Edman degradation
    • Di Maro A, Ferranti P, Mastronicola M, Polito L, Bolognesi A, Stirpe F, Malorni A, Parente A (2001) Reliable sequence determination of ribosome- inactivating proteins by combining electrospray mass spectrometry and Edman degradation. J Mass Spectrom 36: 38-46.
    • (2001) J Mass Spectrom , vol.36 , pp. 38-46
    • Di Maro, A.1    Ferranti, P.2    Mastronicola, M.3    Polito, L.4    Bolognesi, A.5    Stirpe, F.6    Malorni, A.7    Parente, A.8
  • 13
    • 0028133015 scopus 로고
    • Rye inhibitors of animal alpha-amylases show different specificities, aggregative properties and IgE-binding capacities than their homologues from wheat and barley
    • Garcia-Casado G, Sanchez-Monge R, Lopez-Otin C, Salcedo G (1994) Rye inhibitors of animal alpha-amylases show different specificities, aggregative properties and IgE-binding capacities than their homologues from wheat and barley. Eur J Biochem 224: 525-531.
    • (1994) Eur J Biochem , vol.224 , pp. 525-531
    • Garcia-Casado, G.1    Sanchez-Monge, R.2    Lopez-Otin, C.3    Salcedo, G.4
  • 15
    • 0025403113 scopus 로고
    • Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein
    • Gautier MF, Alary R, Joudrier P (1990) Cloning and characterization of a cDNA encoding the wheat (Triticum durum Desf.) CM16 protein. Plant Mol Biol 14: 313-322.
    • (1990) Plant Mol Biol , vol.14 , pp. 313-322
    • Gautier, M.F.1    Alary, R.2    Joudrier, P.3
  • 16
  • 17
    • 0014557349 scopus 로고
    • Alanine p-nitrophenyl esterase activity of human leucocyte granules
    • Janoff A (1969) Alanine p-nitrophenyl esterase activity of human leucocyte granules. Biochem J 114: 157-159.
    • (1969) Biochem J , vol.114 , pp. 157-159
    • Janoff, A.1
  • 18
    • 0030815231 scopus 로고    scopus 로고
    • Tertiary and quaternary structures of 0.19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 Å resolution
    • Oda Y, Matsunaga T, Fukuyama K, Miyazaki T, Morimoto T (1997) Tertiary and quaternary structures of 0. 19 α-amylase inhibitor from wheat kernel determined by X-ray analysis at 2. 06 Å resolution. Biochemistry 36: 13503-13511.
    • (1997) Biochemistry , vol.36 , pp. 13503-13511
    • Oda, Y.1    Matsunaga, T.2    Fukuyama, K.3    Miyazaki, T.4    Morimoto, T.5
  • 19
    • 0020610085 scopus 로고
    • A possible evolutionary relationship between plant trypsin inhibitor, alpha-amylase inhibitor, and mammalian pancreatic secretory trypsin inhibitor (Kazal)
    • Odani S, Koide T, Ono T (1983) A possible evolutionary relationship between plant trypsin inhibitor, alpha-amylase inhibitor, and mammalian pancreatic secretory trypsin inhibitor (Kazal). J Biochem 1993: 1701-1704.
    • (1983) J Biochem , vol.1993 , pp. 1701-1704
    • Odani, S.1    Koide, T.2    Ono, T.3
  • 20
    • 0022432686 scopus 로고
    • Molecular basis of superreactivity of cysteine residues 31 and 32 of seminal ribonuclease
    • Parente A, Merrifield B, Geraci G, D'Alessio G (1985) Molecular basis of superreactivity of cysteine residues 31 and 32 of seminal ribonuclease. Biochemistry 24: 1098-1104.
    • (1985) Biochemistry , vol.24 , pp. 1098-1104
    • Parente, A.1    Merrifield, B.2    Geraci, G.3    D'Alessio, G.4
  • 21
    • 0000679720 scopus 로고
    • A trypsin inhibitor from the water-soluble protein fraction of wheat kernel
    • Poerio E, Carrano L, Carzillo AM, Buonocore V (1989) A trypsin inhibitor from the water-soluble protein fraction of wheat kernel. Phytochemistry 28: 1307-1311.
    • (1989) Phytochemistry , vol.28 , pp. 1307-1311
    • Poerio, E.1    Carrano, L.2    Carzillo, A.M.3    Buonocore, V.4
  • 22
    • 0037300857 scopus 로고    scopus 로고
    • Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin
    • Poerio E, Di Gennaro S, Di Maro A, Farisei F, Ferranti P, Parente A (2003) Primary structure and reactive site of a novel wheat proteinase inhibitor of subtilisin and chymotrypsin. Biol Chem 384: 295-304.
    • (2003) Biol Chem , vol.384 , pp. 295-304
    • Poerio, E.1    Di Gennaro, S.2    Di Maro, A.3    Farisei, F.4    Ferranti, P.5    Parente, A.6
  • 23
    • 51649155466 scopus 로고
    • A rapid method for the quantitative assessment of levels of specific mRNAs in plants
    • Prescott A, Martin C (1987) A rapid method for the quantitative assessment of levels of specific mRNAs in plants. Plant Mol Biol Rep 4: 219-224.
    • (1987) Plant Mol Biol Rep , vol.4 , pp. 219-224
    • Prescott, A.1    Martin, C.2
  • 24
    • 1642464622 scopus 로고    scopus 로고
    • Evolutionary families of peptidase inhibitors
    • Rawlings ND, Tolle DP, Barrett AJ (2004a) Evolutionary families of peptidase inhibitors. Biochem J 378: 705-716.
    • (2004) Biochem J , vol.378 , pp. 705-716
    • Rawlings, N.D.1    Tolle, D.P.2    Barrett, A.J.3
  • 26
    • 0001144526 scopus 로고
    • Seed storage proteins: the enzyme inhibitors
    • In: Rogers LJ (ed) Academic Press, New York
    • Richardson M (1991) Seed storage proteins: the enzyme inhibitors. In: Rogers LJ (ed) Methods in plant biochemistry, vol 5. Academic Press, New York, pp 259-305.
    • (1991) Methods in plant biochemistry , vol.5 , pp. 259-305
    • Richardson, M.1
  • 27
    • 34047263777 scopus 로고    scopus 로고
    • The identification of a barley haze active protein that influences beer haze stability: cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type
    • Robinson LH, Juttner J, Milligan A, Lahnstein J, Eglinton JK, Evans DE (2007) The identification of a barley haze active protein that influences beer haze stability: cloning and characterisation of the barley SE protein as a barley trypsin inhibitor of the chloroform/methanol type. J Cereal Sci 45: 343-352.
    • (2007) J Cereal Sci , vol.45 , pp. 343-352
    • Robinson, L.H.1    Juttner, J.2    Milligan, A.3    Lahnstein, J.4    Eglinton, J.K.5    Evans, D.E.6
  • 29
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 30
    • 0000180578 scopus 로고
    • Protease inhibitors in plants: genes for improving defenses against insects and pathogens
    • Ryan CA (1990) Protease inhibitors in plants: genes for improving defenses against insects and pathogens. Annu Rev Phytopathol 28: 425-449.
    • (1990) Annu Rev Phytopathol , vol.28 , pp. 425-449
    • Ryan, C.A.1
  • 31
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    von Jagow, G.2
  • 34
    • 0028997212 scopus 로고
    • Plant storage proteins
    • Shewry PR (1995) Plant storage proteins. Biol Rev 70: 375-426.
    • (1995) Biol Rev , vol.70 , pp. 375-426
    • Shewry, P.R.1
  • 37
    • 0001745868 scopus 로고    scopus 로고
    • Proteinase inhibitors: plant-derived genes of insecticidal protein for developing insect-resistant transgenic plants
    • Ussuf KK, Laxmi NH, Mitra R (2001) Proteinase inhibitors: plant-derived genes of insecticidal protein for developing insect-resistant transgenic plants. Curr Sci 80: 847-853.
    • (2001) Curr Sci , vol.80 , pp. 847-853
    • Ussuf, K.K.1    Laxmi, N.H.2    Mitra, R.3


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