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Volumn 52, Issue 20, 2004, Pages 6115-6121

Isolation and properties of a Kunitz-type protein inhibitor obtained from Pithecellobium dulce seeds

Author keywords

Cytotoxicity; Kunitz inhibitor; Pithecellobium dulce; Seed protein; Trypsin inhibitor

Indexed keywords

CHYMOTRYPSIN INHIBITOR; PITHECELLOBIUM DULCE EXTRACT; PLANT EXTRACT; POLYPEPTIDE; SERINE PROTEINASE INHIBITOR; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 4744374775     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf049694b     Document Type: Article
Times cited : (25)

References (40)
  • 2
    • 0032487599 scopus 로고    scopus 로고
    • Growth analysis of nine multipurpose woody legumes native from southern Mexico
    • Cervantes, V.; Arriaga, V.; Meave, J.; Carabias, J. Growth analysis of nine multipurpose woody legumes native from southern Mexico. Forest Ecol. Manag. 1998, 110, 329-341.
    • (1998) Forest Ecol. Manag. , vol.110 , pp. 329-341
    • Cervantes, V.1    Arriaga, V.2    Meave, J.3    Carabias, J.4
  • 3
    • 0010366467 scopus 로고    scopus 로고
    • La problemática socioambiental e institucional de la reforestación en la región de La Montaña, Guerrero, Mexico
    • Cervantes, V.; Arriaga, V.; Carabias, J. La problemática socioambiental e institucional de la reforestación en la región de La Montaña, Guerrero, Mexico. Bol. Soc. Bot. Mexico 1996, 59, 67-80.
    • (1996) Bol. Soc. Bot. Mexico , vol.59 , pp. 67-80
    • Cervantes, V.1    Arriaga, V.2    Carabias, J.3
  • 7
    • 0037670129 scopus 로고    scopus 로고
    • Seasonal evaluation of the postharvest fungicidal activity of powders and extracts of huamuchil (Pithecellobium dulce): Action against Botrytis cinerea, Penicillium digitatum and Rhizopus stolonifer of strawberry fruit
    • Bautista-Baños, S.; García-Domínguez, E.; Barrera-Necha, L. L.; Reyes-Chilpa, R.; Wilson, C. L. Seasonal evaluation of the postharvest fungicidal activity of powders and extracts of huamuchil (Pithecellobium dulce): action against Botrytis cinerea, Penicillium digitatum and Rhizopus stolonifer of strawberry fruit. Postharvest Biol. Technol. 2003, 29, 81-92.
    • (2003) Postharvest Biol. Technol. , vol.29 , pp. 81-92
    • Bautista-Baños, S.1    García-Domínguez, E.2    Barrera-Necha, L.L.3    Reyes-Chilpa, R.4    Wilson, C.L.5
  • 10
    • 4744353175 scopus 로고
    • Dietary fiber and starch contents of some southeast Asian vegetables
    • Candlish, J. K.; Gourley, L.; Lee, H. P. Dietary fiber and starch contents of some southeast Asian vegetables. J. Agric. Food Chem. 1987, 35, 319-321.
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 319-321
    • Candlish, J.K.1    Gourley, L.2    Lee, H.P.3
  • 11
    • 0008402861 scopus 로고
    • Legumes and a cereal with high methionine/cysteine contents
    • de Lumen, B. O.; Becker, R.; Reyes, P. S. Legumes and a cereal with high methionine/cysteine contents. J. Agric. Food Chem. 1986, 34, 361-364.
    • (1986) J. Agric. Food Chem. , vol.34 , pp. 361-364
    • De Lumen, B.O.1    Becker, R.2    Reyes, P.S.3
  • 12
    • 0023020554 scopus 로고
    • Protease inhibitors in plant foods: Content and Inactivation
    • Rackis, J. J.; Wolf, W. J.; Backer, E. C. Protease inhibitors in plant foods: Content and Inactivation. Adv. Exp. Med. Biol. 1986, 199, 299-347.
    • (1986) Adv. Exp. Med. Biol. , vol.199 , pp. 299-347
    • Rackis, J.J.1    Wolf, W.J.2    Backer, E.C.3
  • 13
    • 0010751075 scopus 로고
    • Characteristics and fatty acid content of the fat of seeds of nine wild Mexican Plants
    • Sotelo, A.; Lucas, B.; Garza, L.; Giral, F. Characteristics and fatty acid content of the fat of seeds of nine wild Mexican Plants. J. Agric. Food Chem. 1990, 38, 1503-1505.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1503-1505
    • Sotelo, A.1    Lucas, B.2    Garza, L.3    Giral, F.4
  • 14
    • 0000078132 scopus 로고    scopus 로고
    • Enzyme inhibitors of seeds: Types and properties
    • Shewry, P. R., Casey, R., Eds.; Kluwer Academic: Dordrecht, The Netherlands
    • Shewry, P. R. Enzyme inhibitors of seeds: Types and properties. In Protease Inhibitors in Plant: Genes for Improving Defenses against Insects and Pathogens; Shewry, P. R., Casey, R., Eds.; Kluwer Academic: Dordrecht, The Netherlands, 1999; pp 587-615.
    • (1999) Protease Inhibitors in Plant: Genes for Improving Defenses Against Insects and Pathogens , pp. 587-615
    • Shewry, P.R.1
  • 16
    • 0347242675 scopus 로고
    • Nutritional value and content of antinutritional compounds and toxics in 10 wild legumes of Yucatán Peninsula
    • Sotelo, A.; Contreras, E.; Flores, S. Nutritional value and content of antinutritional compounds and toxics in 10 wild legumes of Yucatán Peninsula. Plant Foods Hum. Nutr. 1995, 47, 115-123.
    • (1995) Plant Foods Hum. Nutr. , vol.47 , pp. 115-123
    • Sotelo, A.1    Contreras, E.2    Flores, S.3
  • 17
    • 84988164418 scopus 로고
    • The influence of pea seed trypsin inhibitors on the in vitro digestibility of casein
    • Al-Wesaly, M.; Lambert, N.; Welhman, T.; Domoney, C. The influence of pea seed trypsin inhibitors on the in vitro digestibility of casein. J. Sci. Food Agric. 1995, 68, 431-437.
    • (1995) J. Sci. Food Agric. , vol.68 , pp. 431-437
    • Al-Wesaly, M.1    Lambert, N.2    Welhman, T.3    Domoney, C.4
  • 18
    • 85004399341 scopus 로고
    • Distribution of the Kunitz and the Bowman-Birk family proteinase inhibitors in leguminous seeds
    • Norioka, N.; Hara, S.; Ikenaka, T.; Abe, J. Distribution of the Kunitz and the Bowman-Birk family proteinase inhibitors in leguminous seeds. Agric. Biol. Chem. 1988, 52, 1245-1252.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1245-1252
    • Norioka, N.1    Hara, S.2    Ikenaka, T.3    Abe, J.4
  • 19
    • 0026444760 scopus 로고
    • The presence and inactivation of trypsin inhibitors, tannins, lectins and amylase inhibitors in legume seeds during germination. A review
    • Savelkoul, F. H. M. G.; Van Der Poel, A. F. B.; Tamminga, S. The presence and inactivation of trypsin inhibitors, tannins, lectins and amylase inhibitors in legume seeds during germination. A review. Plant Foods Hum. Nutr. 1992, 42, 71-85.
    • (1992) Plant Foods Hum. Nutr. , vol.42 , pp. 71-85
    • Savelkoul, F.H.M.G.1    Van Der Poel, A.F.B.2    Tamminga, S.3
  • 20
    • 4744356772 scopus 로고    scopus 로고
    • A diffusion of proteinase inhibitors from seeds in process of germination
    • Zainutdinova, G. F.; Ibragimov, R. I. A diffusion of proteinase inhibitors from seeds in process of germination. Plant Physiol. Biochem. 2000, 38, 545.
    • (2000) Plant Physiol. Biochem. , vol.38 , pp. 545
    • Zainutdinova, G.F.1    Ibragimov, R.I.2
  • 21
    • 0031741056 scopus 로고    scopus 로고
    • The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent
    • Kennedy, A. R. The Bowman-Birk inhibitor from soybeans as an anticarcinogenic agent. Am. J. Clin. Nutr. 1998, 68, 1406S-1412S.
    • (1998) Am. J. Clin. Nutr. , vol.68
    • Kennedy, A.R.1
  • 22
    • 0027728297 scopus 로고
    • Purification, characterization, and complete amino acid sequence of a trypsin inhibitor from amaranth (Amaranthus hypochondriacus) seeds
    • Valdez-Rodríguez, S.; Segura-Nieto, M.; Chagolla-Lopez, A.; Verver, A.; Martinez-Gallardo, N.; Blanco-Labra, A. Purification, characterization, and complete amino acid sequence of a trypsin inhibitor from amaranth (Amaranthus hypochondriacus) seeds. Plant Physiol. 1993, 103, 1407-1412.
    • (1993) Plant Physiol. , vol.103 , pp. 1407-1412
    • Valdez-Rodríguez, S.1    Segura-Nieto, M.2    Chagolla-Lopez, A.3    Verver, A.4    Martinez-Gallardo, N.5    Blanco-Labra, A.6
  • 23
    • 1542652441 scopus 로고
    • A spectrophotometric determination of trypsin and chymotrypsin activity
    • Schwert, G. W.; Takenaka, Y. A spectrophotometric determination of trypsin and chymotrypsin activity. Biochim. Biophys. Acta 1955, 16, 571-575.
    • (1955) Biochim. Biophys. Acta , vol.16 , pp. 571-575
    • Schwert, G.W.1    Takenaka, Y.2
  • 24
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H.; Von-Jagow, G. Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von-Jagow, G.2
  • 25
    • 84988074679 scopus 로고
    • Improved silver staining of plant protein, RNA and DNA in polyacrylamide gels
    • Bloom, H.; Beier, H.; Gross, H. S. Improved silver staining of plant protein, 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.S.3
  • 27
    • 0026330761 scopus 로고
    • S. Trypsin inhibitor from the seeds of Acacia confusa
    • Lin, J. Y.; Chu, S. c.; Wu, H.; Hsieh, Y. S. Trypsin inhibitor from the seeds of Acacia confusa. J. Biochem. 1991, 110, 879-883.
    • (1991) J. Biochem. , vol.110 , pp. 879-883
    • Lin, J.Y.1    Chu, S.C.2    Wu, H.3    Hsieh, Y.4
  • 29
    • 0018557628 scopus 로고
    • Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz)
    • Odani, S.; Odani, S.; Ono, T.; Ikenaka, T. Proteinase inhibitors from a mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz). J. Biochem. 1979, 86, 1795-1805.
    • (1979) J. Biochem. , vol.86 , pp. 1795-1805
    • Odani, S.1    Odani, S.2    Ono, T.3    Ikenaka, T.4
  • 30
    • 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.). BBA-Protein Struct. Mol. Enzymol. 1986, 872, 134-140.
    • (1986) BBA-Protein Struct. Mol. Enzymol. , 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
  • 31
    • 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
  • 32
    • 0037110544 scopus 로고    scopus 로고
    • Overlapping binding sites for trypsin and papain on Kunitz-type proteinase inhibitor from Prospis juliflora
    • Franco, O. L.; Grossi de Sá, M. F.; Sales, M. P.; Mello, L. V.; Oliveira, A. S.; Rigden, D. J. Overlapping binding sites for trypsin and papain on Kunitz-type proteinase inhibitor from Prospis juliflora. Proteins 2002, 49, 335-341.
    • (2002) Proteins , vol.49 , pp. 335-341
    • Franco, O.L.1    Grossi De Sá, M.F.2    Sales, M.P.3    Mello, L.V.4    Oliveira, A.S.5    Rigden, D.J.6
  • 34
    • 0009611219 scopus 로고
    • Continuous, clonar, insulin- and somatostatin-secreting cell lines established from a transplantable rat islet cell tumor
    • Gazdar, A.; Chick, W.; Sims, H.; King, D.; Weir, G.; Lauris, V. Continuous, clonar, insulin- and somatostatin-secreting cell lines established from a transplantable rat islet cell tumor. Proc. Natl. Acad. Sci. U.S.A. 1980, 77, 3519-3523.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 3519-3523
    • Gazdar, A.1    Chick, W.2    Sims, H.3    King, D.4    Weir, G.5    Lauris, V.6
  • 35
    • 0031782418 scopus 로고    scopus 로고
    • Chemopreventive agents: Protease inhibitors
    • Kennedy, A. R. Chemopreventive agents: Protease inhibitors. Pharmacol Ther. 1998, 78, 167-209.
    • (1998) Pharmacol Ther. , vol.78 , pp. 167-209
    • Kennedy, A.R.1
  • 36
    • 0037452941 scopus 로고    scopus 로고
    • Anticarcinogenic Bowman Birk inhibitor from snail medic seeds (Medicago scutellata): Solution structure and analysis of self-association behavior
    • Catalane, M.; Ragona, I.; Molinari, H.; Tava, A.; Zetta, L. Anticarcinogenic Bowman Birk inhibitor from snail medic seeds (Medicago scutellata): Solution structure and analysis of self-association behavior. Biochemistry 2003, 42, 2836-2846.
    • (2003) Biochemistry , vol.42 , pp. 2836-2846
    • Catalane, M.1    Ragona, I.2    Molinari, H.3    Tava, A.4    Zetta, L.5
  • 38
    • 0033578756 scopus 로고    scopus 로고
    • Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma
    • Wilharm, E.; Parry, M. A. A.; Friebel, R.; Tschesche, H.; Matschiner, G.; Sommerhoff, C. P.; Jenne, D. E. Generation of catalytically active granzyme K from Escherichia coli inclusion bodies and identification of efficient granzyme K inhibitors in human plasma. J. Biol. Chem. 1999, 274, 27331-27337.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27331-27337
    • Wilharm, E.1    Parry, M.A.A.2    Friebel, R.3    Tschesche, H.4    Matschiner, G.5    Sommerhoff, C.P.6    Jenne, D.E.7
  • 39
    • 0035910565 scopus 로고    scopus 로고
    • Suppression of urokinase expression and invasiveness by urinary trypsin inhibitor is mediated through inhibition of protein kinase C- and MEK/ERK/c-Jun-dependent signaling pathways
    • Kobayashi, H.; Suzuki, M.; Tanaka, Y.; Hirashima, Y.; Terao, T. Suppression of urokinase expression and invasiveness by urinary trypsin inhibitor is mediated through inhibition of protein kinase C- and MEK/ERK/c-Jun-dependent signaling pathways. J. Biol. Chem. 2001, 276, 2015-2022.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2015-2022
    • Kobayashi, H.1    Suzuki, M.2    Tanaka, Y.3    Hirashima, Y.4    Terao, T.5
  • 40
    • 0037424469 scopus 로고    scopus 로고
    • A Kunitz-type protease inhibitor, bikunin, inhibits ovarian cancer cell invasion by blocking the calcium-dependent transforming growth factor-β1 signaling cascade
    • Kobayashi, H.; Suzuki, M.; Tanaka, Y.; Kanayama, N.; Terao, T. A Kunitz-type protease inhibitor, bikunin, inhibits ovarian cancer cell invasion by blocking the calcium-dependent transforming growth factor-β1 signaling cascade. J. Biol. Chem. 2003, 278, 7790-7799.
    • (2003) J. Biol. Chem. , vol.278 , pp. 7790-7799
    • Kobayashi, H.1    Suzuki, M.2    Tanaka, Y.3    Kanayama, N.4    Terao, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.