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Volumn 70, Issue 7, 2009, Pages 871-879

Physico-chemical and antifungal properties of protease inhibitors from Acacia plumosa

Author keywords

Acacia plumosa; Antifungal activity; Kunitz type protease inhibitor; Leguminosae; Surface plasmon resonance

Indexed keywords

ANTIFUNGAL AGENT; APROTININ; CHYMOTRYPSIN; TRYPSIN;

EID: 67249121053     PISSN: 00319422     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.phytochem.2009.04.009     Document Type: Article
Times cited : (73)

References (40)
  • 2
    • 26844473090 scopus 로고    scopus 로고
    • Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies
    • Araújo A.P.U., Hansen D., Vieira D.F., Oliveira C., Santana L.A., Beltramini L.M., Sampaio C.A.M., and Oliva M.L.V. Kunitz-type Bauhinia bauhinioides inhibitors devoid of disulfide bridges: isolation of the cDNAs, heterologous expression and structural studies. Biol. Chem. 386 (2005) 561-568
    • (2005) Biol. Chem. , vol.386 , pp. 561-568
    • Araújo, A.P.U.1    Hansen, D.2    Vieira, D.F.3    Oliveira, C.4    Santana, L.A.5    Beltramini, L.M.6    Sampaio, C.A.M.7    Oliva, M.L.V.8
  • 3
    • 2142714477 scopus 로고    scopus 로고
    • Antibacterial activity of ethanolic and aqueous extracts of Acacia aroma Gill. ex Hook et Arn
    • Arias M.E., Gomez J.D., Cudmani N.M., Vattuone M.A., and Isla M.I. Antibacterial activity of ethanolic and aqueous extracts of Acacia aroma Gill. ex Hook et Arn. Life Sci. 75 (2004) 191-202
    • (2004) Life Sci. , vol.75 , pp. 191-202
    • Arias, M.E.1    Gomez, J.D.2    Cudmani, N.M.3    Vattuone, M.A.4    Isla, M.I.5
  • 6
    • 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., and Babu C.R. A Kunitz proteinase inhibitor from Archidendron ellipticum seeds: purification, characterization, and kinetic properties. Phytochemistry 67 3 (2006) 232-241
    • (2006) Phytochemistry , vol.67 , Issue.3 , pp. 232-241
    • Bhattacharyya, A.1    Mazumdar, S.2    Leighton, S.M.3    Babu, C.R.4
  • 7
    • 67249143906 scopus 로고    scopus 로고
    • Brady, R.L., 2003. Plant Protease Inhibitors: Significance In Nutrition, Plant Protection, Cancer Prevention and Genetic Engineering pp. 170 (2003. Phytochemistry 64 (8), 1419).
    • Brady, R.L., 2003. Plant Protease Inhibitors: Significance In Nutrition, Plant Protection, Cancer Prevention and Genetic Engineering pp. 170 (2003. Phytochemistry 64 (8), 1419).
  • 8
    • 2342525840 scopus 로고    scopus 로고
    • A classification of plant food allergens
    • Breiteneder H., and Radauer C. A classification of plant food allergens. J. Allergy Clin. Immun. 113 5 (2004) 821-830
    • (2004) J. Allergy Clin. Immun. , vol.113 , Issue.5 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.2
  • 9
    • 0015794613 scopus 로고
    • Fluorescence and the location of tryptophan residues in protein molecules
    • Burstein E.A., Vedenkina N.S., and Ivkova M.N. Fluorescence and the location of tryptophan residues in protein molecules. Photochem. Photobiol. 18 (1973) 263-279
    • (1973) Photochem. Photobiol. , vol.18 , pp. 263-279
    • Burstein, E.A.1    Vedenkina, N.S.2    Ivkova, M.N.3
  • 10
    • 0036842625 scopus 로고    scopus 로고
    • Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides
    • Carlini C.R., and Grossi-de-Sá M.F. Plant toxic proteins with insecticidal properties. A review on their potentialities as bioinsecticides. Toxicon 40 (2002) 1515-1539
    • (2002) Toxicon , vol.40 , pp. 1515-1539
    • Carlini, C.R.1    Grossi-de-Sá, M.F.2
  • 12
    • 0030120446 scopus 로고    scopus 로고
    • The distribution and phylogenetic significance of a 50-kb chloroplast DNA inversion in the flowering plant family Leguminosae
    • Doyle J.J., Doyle J.L., Ballenger J.A., and Palmer J.D. The distribution and phylogenetic significance of a 50-kb chloroplast DNA inversion in the flowering plant family Leguminosae. Mol. Phylogenet. Evol. 5 2 (1996) 429-438
    • (1996) Mol. Phylogenet. Evol. , vol.5 , Issue.2 , pp. 429-438
    • Doyle, J.J.1    Doyle, J.L.2    Ballenger, J.A.3    Palmer, J.D.4
  • 13
    • 0014939933 scopus 로고
    • The chromatographic determination of cystine and cysteine residues in proteins as S-h-(4-Pyridylethyl) cysteine
    • Friedman M., Krull L.H., and Cavins J.F. The chromatographic determination of cystine and cysteine residues in proteins as S-h-(4-Pyridylethyl) cysteine. J. Biol. Chem. 245 (1970) 3868-3871
    • (1970) J. Biol. Chem. , vol.245 , pp. 3868-3871
    • Friedman, M.1    Krull, L.H.2    Cavins, J.F.3
  • 14
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests and pathogens: natural and engineered phytoprojection
    • Haq S.K., Atif S.M., and Khan R.H. Protein proteinase inhibitor genes in combat against insects, pests and pathogens: natural and engineered phytoprojection. Arch. Biochem. Biophys. 431 1 (2004) 145-159
    • (2004) Arch. Biochem. Biophys. , vol.431 , Issue.1 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 15
    • 0348109377 scopus 로고    scopus 로고
    • Characterization of a proteinase inhibitor from Cajanus cajan (L.)
    • Haq S.K., and Khan R.H. Characterization of a proteinase inhibitor from Cajanus cajan (L.). J. Protein Chem. 22 6 (2003) 543-554
    • (2003) J. Protein Chem. , vol.22 , Issue.6 , pp. 543-554
    • Haq, S.K.1    Khan, R.H.2
  • 16
    • 0024234855 scopus 로고
    • CLUSTAL: a package for performing multiple sequence alignment on a microcomputer
    • Higgins D.G., and Sharp P.M. CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73 1 (1988) 237-244
    • (1988) Gene , vol.73 , Issue.1 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 17
    • 0027193472 scopus 로고
    • Clonning and expression of the gene encoding Acacia confusa trypsin inhibitor that is active without post-translational proteolysis
    • Hung C.H., Lee M.C., Lin M.T., and Lin J.Y. Clonning and expression of the gene encoding Acacia confusa trypsin inhibitor that is active without post-translational proteolysis. Gene 127 (1993) 215-219
    • (1993) Gene , vol.127 , pp. 215-219
    • Hung, C.H.1    Lee, M.C.2    Lin, M.T.3    Lin, J.Y.4
  • 18
    • 0009382325 scopus 로고
    • Purification and properties of the proteinase inhibitors from Acacia sieberana (paperback Acacia) seed
    • Joubert F.J. Purification and properties of the proteinase inhibitors from Acacia sieberana (paperback Acacia) seed. Phytochemistry 22 (1983) 53-57
    • (1983) Phytochemistry , vol.22 , pp. 53-57
    • Joubert, F.J.1
  • 19
    • 16244401969 scopus 로고    scopus 로고
    • Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato
    • Kim J.Y., Park S.C., Kim M.H., Lim H.T., Park Y., and Hahm K.S. Antimicrobial activity studies on a trypsin-chymotrypsin protease inhibitor obtained from potato. Biochem. Bioph. Res. Co. 330 3 (2005) 921-927
    • (2005) Biochem. Bioph. Res. Co. , vol.330 , Issue.3 , pp. 921-927
    • Kim, J.Y.1    Park, S.C.2    Kim, M.H.3    Lim, H.T.4    Park, Y.5    Hahm, K.S.6
  • 20
    • 0002978054 scopus 로고
    • The characterization of enzyme inhibition
    • Barret, Salvensen Eds, Cambridge. pp
    • Knight, C.G., 1986. The characterization of enzyme inhibition. In: Barret, Salvensen (Eds.), Proteinase Inhibitors. Cambridge. pp. 23-51.
    • (1986) Proteinase Inhibitors , pp. 23-51
    • Knight, C.G.1
  • 21
    • 0019555769 scopus 로고
    • Acacia proteinase inhibitors
    • Kortt A.A., and Jermyn M.A. Acacia proteinase inhibitors. Eur. J. Biochem. 115 (1981) 551-557
    • (1981) Eur. J. Biochem. , vol.115 , pp. 551-557
    • Kortt, A.A.1    Jermyn, M.A.2
  • 22
    • 0000997835 scopus 로고
    • Crystallization of a trypsin inhibitor from soybean
    • Kunitz M. Crystallization of a trypsin inhibitor from soybean. Science 101 (1945) 668-669
    • (1945) Science , vol.101 , pp. 668-669
    • Kunitz, M.1
  • 23
    • 0001943903 scopus 로고    scopus 로고
    • Fluorescence spectroscopy in peptide and protein analysis
    • R.A. Meyers Ed
    • Ladoklhin, A.S., 2000. Fluorescence spectroscopy in peptide and protein analysis. In: R.A. Meyers (Ed.), Encyclopedia of Analytical Chemistry. pp. 5762-5779.
    • (2000) Encyclopedia of Analytical Chemistry , pp. 5762-5779
    • Ladoklhin, A.S.1
  • 24
    • 0026330761 scopus 로고
    • Trypsin inhibitor from the seeds of Acacia confusa
    • Lin J.Y., Chu S.C., Wu H.C., and Hsieh Y.S. Trypsin inhibitor from the seeds of Acacia confusa. J. Biochem. 110 (1991) 879-883
    • (1991) J. Biochem. , vol.110 , pp. 879-883
    • Lin, J.Y.1    Chu, S.C.2    Wu, H.C.3    Hsieh, Y.S.4
  • 26
    • 33745197770 scopus 로고    scopus 로고
    • Identification and stability of trypsin inhibitor isoforms in pea (Pisum sativum L.) cultivars grown in New Zealand
    • Morrison S.C., Savage G.P., Morton J.D., and Russell A.C. Identification and stability of trypsin inhibitor isoforms in pea (Pisum sativum L.) cultivars grown in New Zealand. Food Chem. 100 1 (2007) 1-7
    • (2007) Food Chem. , vol.100 , Issue.1 , pp. 1-7
    • Morrison, S.C.1    Savage, G.P.2    Morton, J.D.3    Russell, A.C.4
  • 27
  • 28
    • 0018557628 scopus 로고
    • Proteinase inhibitors from a Mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz)
    • Odani S., Odani S., Ono T., and Ikenaka T. Proteinase inhibitors from a Mimosoideae legume, Albizzia julibrissin. Homologues of soybean trypsin inhibitor (Kunitz). J. Biochem. 86 6 (1979) 1795-1805
    • (1979) J. Biochem. , vol.86 , Issue.6 , pp. 1795-1805
    • Odani, S.1    Odani, S.2    Ono, T.3    Ikenaka, T.4
  • 30
    • 0031985947 scopus 로고    scopus 로고
    • Cytotoxic activity of selected plants used as antitumorals in Mexican traditional medicine
    • Popoca J., Aguilar A., Alonso D., and Villarreal M.L. Cytotoxic activity of selected plants used as antitumorals in Mexican traditional medicine. J. Ethnopharmacol. 59 (1998) 173-177
    • (1998) J. Ethnopharmacol. , vol.59 , pp. 173-177
    • Popoca, J.1    Aguilar, A.2    Alonso, D.3    Villarreal, M.L.4
  • 31
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers J.C., Asgian J.L., Ekici O.D., and James K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102 (2002) 4639-4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 32
    • 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., and Jagow G.V. Tricine-sodium dodecyl sulfate-polyacrilamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166 (1987) 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Jagow, G.V.2
  • 33
    • 0034802540 scopus 로고    scopus 로고
    • Enzyme mechanism and catalytic property of β propeller phytase
    • Shin S., Ha N.C., Oh B.C., Oh T.K., and Oh B.H. Enzyme mechanism and catalytic property of β propeller phytase. Structure 9 9 (2001) 851-858
    • (2001) Structure , vol.9 , Issue.9 , pp. 851-858
    • Shin, S.1    Ha, N.C.2    Oh, B.C.3    Oh, T.K.4    Oh, B.H.5
  • 34
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.W.2
  • 35
    • 0037302324 scopus 로고    scopus 로고
    • Structural composition of βI and βII-proteins
    • Sreerama N., and Woody R.W. Structural composition of βI and βII-proteins. Protein Sci. 12 (2003) 384-388
    • (2003) Protein Sci. , vol.12 , pp. 384-388
    • Sreerama, N.1    Woody, R.W.2
  • 36
    • 32644483711 scopus 로고    scopus 로고
    • Correlating the fractional inhibition of caspase-3 in NT2 cells with apoptotic markers using an active-caspase-3 enzyme-linked immunosorbent assay
    • Tawa P., Giroux A., Grimm E., Han Y., Nicholson D.W., and Xanthoudakis S. Correlating the fractional inhibition of caspase-3 in NT2 cells with apoptotic markers using an active-caspase-3 enzyme-linked immunosorbent assay. Anal. Biochem. 350 1 (2006) 32-40
    • (2006) Anal. Biochem. , vol.350 , Issue.1 , pp. 32-40
    • Tawa, P.1    Giroux, A.2    Grimm, E.3    Han, Y.4    Nicholson, D.W.5    Xanthoudakis, S.6
  • 37
    • 1842767175 scopus 로고    scopus 로고
    • Purifications and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds
    • Teles R.C.L., Souza E.M.T., Calderon L.A., and Freitas S.M. Purifications and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds. Phytochemistry 65 (2004) 793-799
    • (2004) Phytochemistry , vol.65 , pp. 793-799
    • Teles, R.C.L.1    Souza, E.M.T.2    Calderon, L.A.3    Freitas, S.M.4
  • 39
    • 0017822448 scopus 로고
    • Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins
    • Woody R.W. Aromatic side-chain contributions to the far ultraviolet circular dichroism of peptides and proteins. Biopolymers 17 (1978) 451-467
    • (1978) Biopolymers , vol.17 , pp. 451-467
    • Woody, R.W.1
  • 40
    • 30144438891 scopus 로고    scopus 로고
    • Update on HAART in HIV
    • Yeni P. Update on HAART in HIV. J. Hepatol. 44 1 (2006) 100-103
    • (2006) J. Hepatol. , vol.44 , Issue.1 , pp. 100-103
    • Yeni, P.1


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