메뉴 건너뛰기




Volumn 2010, Issue , 2010, Pages

Trypsin isoinhibitors with antiproliferative activity toward leukemia cells from phaseolus vulgaris cv "white cloud bean"

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; DITHIOTHREITOL; PHASEOLUS VULGARIS EXTRACT; PLANT EXTRACT; RNA DIRECTED DNA POLYMERASE; THYMIDINE; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG; INTEGRASE; P31 INTEGRASE PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; VEGETABLE PROTEIN;

EID: 77954548260     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2010/219793     Document Type: Article
Times cited : (12)

References (65)
  • 2
    • 0032537818 scopus 로고    scopus 로고
    • The spectroscopic analysis, inhibition and binding studies demonstrate the equivalence of Erythrina caffra trypsin inhibitor and the recombinant substitution variant recSerETI
    • Minuth T., Krmer B., Lehle K., Jaenicke R., Kohnert U., The spectroscopic analysis, inhibition and binding studies demonstrate the equivalence of Erythrina caffra trypsin inhibitor and the recombinant substitution variant recSerETI Journal of Biotechnology 1998 62 3 231 239
    • (1998) Journal of Biotechnology , vol.62 , Issue.3 , pp. 231-239
    • Minuth, T.1    Krmer, B.2    Lehle, K.3    Jaenicke, R.4    Kohnert, U.5
  • 3
    • 53149104002 scopus 로고    scopus 로고
    • Purification and characterization of a proteinase inhibitor from field bean, Dolichos lablab perpureus L
    • Devaraj V. R., Manjunatha N. H., Purification and characterization of a proteinase inhibitor from field bean, Dolichos lablab perpureus L Journal of Protein Chemistry 1999 18 1 47 54
    • (1999) Journal of Protein Chemistry , vol.18 , Issue.1 , pp. 47-54
    • Devaraj, V.R.1    Manjunatha, N.H.2
  • 4
    • 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 5 519 523
    • (1999) IUBMB Life , vol.48 , Issue.5 , 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
  • 7
    • 0034297354 scopus 로고    scopus 로고
    • Complete amino acid sequences of three proteinase inhibitors from white sword bean (Canavalia gladiata)
    • Park S.-S., Sumi T., Ohba H., Nakamura O., Kimura M., Complete amino acid sequences of three proteinase inhibitors from white sword bean (Canavalia gladiata) Bioscience, Biotechnology and Biochemistry 2000 64 10 2272 2275
    • (2000) Bioscience, Biotechnology and Biochemistry , vol.64 , Issue.10 , pp. 2272-2275
    • Park, S.-S.1    Sumi, T.2    Ohba, H.3    Nakamura, O.4    Kimura, M.5
  • 8
    • 0142135609 scopus 로고    scopus 로고
    • PA1b, an insecticidal protein extracted from pea seeds (Pisum sativum): 1H-2-D NMR study and molecular modeling
    • Jouvensal L., Quillien L., Ferrasson E., Rahb Y., Guguen J., Vovelle F., PA1b, an insecticidal protein extracted from pea seeds (Pisum sativum): 1H-2-D NMR study and molecular modeling Biochemistry 2003 42 41 11915 11923
    • (2003) Biochemistry , vol.42 , Issue.41 , pp. 11915-11923
    • Jouvensal, L.1    Quillien, L.2    Ferrasson, E.3    Rahb, Y.4    Guguen, J.5    Vovelle, F.6
  • 13
    • 16544377766 scopus 로고    scopus 로고
    • Trypsin inhibitor from Poecilanthe parviflora seeds: Purification, characterization, and activity against pest proteases
    • Garcia V. A., Freire M. D. G. M., Novello J. C., Marangoni S., Macedo M. L. R., Trypsin inhibitor from Poecilanthe parviflora seeds: purification, characterization, and activity against pest proteases Protein Journal 2004 23 5 343 350
    • (2004) Protein Journal , vol.23 , Issue.5 , pp. 343-350
    • Garcia, V.A.1    Freire, M.D.G.M.2    Novello, J.C.3    Marangoni, S.4    MacEdo, M.L.R.5
  • 14
    • 2342519504 scopus 로고    scopus 로고
    • A Kunitz-type inhibitor of coleopteran proteases, isolated from adenanthera pavonina L. seeds and its effect on Callosobruchus maculatus
    • Macedo M. L. R., De S C. M., Freire M. D. G. M., Parra J. R. P., A Kunitz-type inhibitor of coleopteran proteases, isolated from adenanthera pavonina L. seeds and its effect on Callosobruchus maculatus Journal of Agricultural and Food Chemistry 2004 52 9 2533 2540
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.9 , pp. 2533-2540
    • MacEdo, M.L.R.1    De S, C.M.2    Freire, M.D.G.M.3    Parra, J.R.P.4
  • 15
    • 0348109377 scopus 로고    scopus 로고
    • Characterization of a Proteinase Inhibitor from Cajanus cajan (L.)
    • Haq S. K., Khan R. H., Characterization of a Proteinase Inhibitor from Cajanus cajan (L.) Journal of Protein Chemistry 2003 22 6 543 554
    • (2003) Journal of Protein Chemistry , vol.22 , Issue.6 , pp. 543-554
    • Haq, S.K.1    Khan, R.H.2
  • 16
    • 0035983827 scopus 로고    scopus 로고
    • Formation of Bowman-Birk inhibitors during the germination of horsegram (Dolichos biflorus)
    • Kumar P., Sreerama Y. N., Gowda L. R., Formation of Bowman-Birk inhibitors during the germination of horsegram (Dolichos biflorus) Phytochemistry 2002 60 6 581 588
    • (2002) Phytochemistry , vol.60 , Issue.6 , pp. 581-588
    • Kumar, P.1    Sreerama, Y.N.2    Gowda, L.R.3
  • 17
    • 1842587836 scopus 로고    scopus 로고
    • Unusual structural characteristics and complete amino acid sequence of a protease inhibitor from Phaseolus acutifolius seeds
    • Campos J. E., Whitaker J. R., Yip T.-T., Hutchens T. W., Blanco-Labra A., Unusual structural characteristics and complete amino acid sequence of a protease inhibitor from Phaseolus acutifolius seeds Plant Physiology and Biochemistry 2004 42 3 209 214
    • (2004) Plant Physiology and Biochemistry , vol.42 , Issue.3 , pp. 209-214
    • Campos, J.E.1    Whitaker, J.R.2    Yip, T.-T.3    Hutchens, T.W.4    Blanco-Labra, A.5
  • 18
    • 1542317102 scopus 로고    scopus 로고
    • CDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4
    • Dodo H. W., Viquez O. M., Maleki S. J., Konan K. N., cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4 Journal of Agricultural and Food Chemistry 2004 52 5 1404 1409
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.5 , pp. 1404-1409
    • Dodo, H.W.1    Viquez, O.M.2    Maleki, S.J.3    Konan, K.N.4
  • 19
    • 1642578980 scopus 로고    scopus 로고
    • Molecular mechanism of enzyme inhibition: Prediction of the three-dimensional structure of the dimeric trypsin inhibitor from Leucaena leucocephala by homology modelling
    • Sattar R., Ali S. A., Kamal M., Khan A. A., Abbasi A., Molecular mechanism of enzyme inhibition: prediction of the three-dimensional structure of the dimeric trypsin inhibitor from Leucaena leucocephala by homology modelling Biochemical and Biophysical Research Communications 2004 314 3 755 765
    • (2004) Biochemical and Biophysical Research Communications , vol.314 , Issue.3 , pp. 755-765
    • Sattar, R.1    Ali, S.A.2    Kamal, M.3    Khan, A.A.4    Abbasi, A.5
  • 20
    • 0032706011 scopus 로고    scopus 로고
    • Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: Inhibition of the hydrolysis of kininogen related substrates
    • Oliva M. L. V., R. Mendes C., Juliano M. A., Chagas J. R., Rosa J. C., Greene L. J., Sampaio M. U., Sampaio C. A. M., Characterization of a tissue kallikrein inhibitor isolated from Bauhinia bauhinioides seeds: inhibition of the hydrolysis of kininogen related substrates Immunopharmacology 1999 45 13 163 169
    • (1999) Immunopharmacology , vol.45 , Issue.13 , pp. 163-169
    • Oliva, M.L.V.1    Mendes, C.R.2    Juliano, M.A.3    Chagas, J.R.4    Rosa, J.C.5    Greene, L.J.6    Sampaio, M.U.7    Sampaio, C.A.M.8
  • 22
    • 0032733732 scopus 로고    scopus 로고
    • Human plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolated from Bauhinia ungulata seeds
    • Oliva M. L. V., Andrade S., Batista I. F. C., Sampaio M. U., Juliano M., Fritz H., Auerswald E. A., Sampaio C. A. M., Human plasma kallikrein and tissue kallikrein binding to a substrate based on the reactive site of a factor Xa inhibitor isolated from Bauhinia ungulata seeds Immunopharmacology 1999 45 13 145 149
    • (1999) Immunopharmacology , vol.45 , Issue.13 , pp. 145-149
    • Oliva, M.L.V.1    Andrade, S.2    Batista, I.F.C.3    Sampaio, M.U.4    Juliano, M.5    Fritz, H.6    Auerswald, E.A.7    Sampaio, C.A.M.8
  • 23
    • 0033231127 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds
    • Rao K. N., Hegde S. S., Lewis R. J., Suresh C. G., Crystallization and preliminary X-ray diffraction studies of a Bowman-Birk inhibitor from Vigna unguiculata seeds Acta Crystallographica Section D 1999 55 11 1920 1922
    • (1999) Acta Crystallographica Section D , vol.55 , Issue.11 , pp. 1920-1922
    • Rao, K.N.1    Hegde, S.S.2    Lewis, R.J.3    Suresh, C.G.4
  • 24
    • 3042654853 scopus 로고    scopus 로고
    • Complete amino acid sequence of the lentil trypsin-chymotrypsin inhibitor LCI-1.7 and a discussion of atypical binding sites of Bowman-Birk inhibitors
    • Weder J. K. P., Hinkers S. C., Complete amino acid sequence of the lentil trypsin-chymotrypsin inhibitor LCI-1.7 and a discussion of atypical binding sites of Bowman-Birk inhibitors Journal of Agricultural and Food Chemistry 2004 52 13 4219 4226
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.13 , pp. 4219-4226
    • Weder, J.K.P.1    Hinkers, S.C.2
  • 26
    • 0037370213 scopus 로고    scopus 로고
    • A novel trypsin inhibitor from Peltophorum dubium seeds, with lectin-like properties, triggers rat lymphoma cell apoptosis
    • Troncoso M. F., Zolezzi P. C., Hellman U., Wolfenstein-Todel C., A novel trypsin inhibitor from Peltophorum dubium seeds, with lectin-like properties, triggers rat lymphoma cell apoptosis Archives of Biochemistry and Biophysics 2003 411 1 93 104
    • (2003) Archives of Biochemistry and Biophysics , vol.411 , Issue.1 , pp. 93-104
    • Troncoso, M.F.1    Zolezzi, P.C.2    Hellman, U.3    Wolfenstein-Todel, C.4
  • 29
    • 0023652256 scopus 로고
    • Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds
    • McPhalen C. A., James M. N. G., Crystal and molecular structure of the serine proteinase inhibitor CI-2 from barley seeds Biochemistry 1987 26 1 261 269
    • (1987) Biochemistry , vol.26 , Issue.1 , pp. 261-269
    • McPhalen, C.A.1    James, M.N.G.2
  • 32
    • 5344259633 scopus 로고    scopus 로고
    • Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: Natural and engineered phytoprotection
    • Haq S. K., Atif S. M., Khan R. H., Protein proteinase inhibitor genes in combat against insects, pests, and pathogens: natural and engineered phytoprotection Archives of Biochemistry and Biophysics 2004 431 1 145 159
    • (2004) Archives of Biochemistry and Biophysics , vol.431 , Issue.1 , pp. 145-159
    • Haq, S.K.1    Atif, S.M.2    Khan, R.H.3
  • 33
    • 0035138276 scopus 로고    scopus 로고
    • Effect of dietary cowpea trypsin inhibitor (CpTI) on the growth and development of the tomato moth Lacanobia oleracea (Lepidoptera: Noctuidae) and on the success of the gregarious ectoparasitoid Eulophus pennicornis (Hymenoptera: Eulophidae)
    • Bell H. A., Fitches E. C., Down R. E., Ford L., Marris G. C., Edwards J. P., Gatehouse J. A., Gatehouse A. M. R., Effect of dietary cowpea trypsin inhibitor (CpTI) on the growth and development of the tomato moth Lacanobia oleracea (Lepidoptera: Noctuidae) and on the success of the gregarious ectoparasitoid Eulophus pennicornis (Hymenoptera: Eulophidae) Pest Management Science 2001 57 1 57 65
    • (2001) Pest Management Science , vol.57 , Issue.1 , pp. 57-65
    • Bell, H.A.1    Fitches, E.C.2    Down, R.E.3    Ford, L.4    Marris, G.C.5    Edwards, J.P.6    Gatehouse, J.A.7    Gatehouse, A.M.R.8
  • 34
    • 0036714821 scopus 로고    scopus 로고
    • Putative protein digestion in a sap-sucking homopteran plant pest (rice brown plant hopper; Nilaparvata lugens: Delphacidae)identification of trypsin-like and cathepsin B-like proteases
    • Foissac X., Edwards M. G., Du J. P., Gatehouse A. M. R., Gatehouse J. A., Putative protein digestion in a sap-sucking homopteran plant pest (rice brown plant hopper; Nilaparvata lugens: Delphacidae)identification of trypsin-like and cathepsin B-like proteases Insect Biochemistry and Molecular Biology 2002 32 9 967 978
    • (2002) Insect Biochemistry and Molecular Biology , vol.32 , Issue.9 , pp. 967-978
    • Foissac, X.1    Edwards, M.G.2    Du, J.P.3    Gatehouse, A.M.R.4    Gatehouse, J.A.5
  • 36
    • 0015433890 scopus 로고
    • Effects of protease inhibitors on growth of hamster tumor cells in culture
    • Goetz I. E., Weinstein C., Roberts E., Effects of protease inhibitors on growth of hamster tumor cells in culture Cancer Research 1972 32 11 2469 2474
    • (1972) Cancer Research , vol.32 , Issue.11 , pp. 2469-2474
    • Goetz, I.E.1    Weinstein, C.2    Roberts, E.3
  • 37
    • 0025945685 scopus 로고
    • Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor
    • von Hofe E., Newberne P. M., Kennedy A. R., Inhibition of N-nitrosomethylbenzylamine-induced esophageal neoplasms by the Bowman-Birk protease inhibitor Carcinogenesis 1991 12 11 2147 2150
    • (1991) Carcinogenesis , vol.12 , Issue.11 , pp. 2147-2150
    • Von Hofe, E.1    Newberne, P.M.2    Kennedy, A.R.3
  • 38
    • 0027318686 scopus 로고
    • Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA
    • Kennedy A. R., Billings P. C., Maki P. A., Newberne P., Effects of various preparations of dietary protease inhibitors on oral carcinogenesis in hamsters induced by DMBA Nutrition and Cancer 1993 19 2 191 200
    • (1993) Nutrition and Cancer , vol.19 , Issue.2 , pp. 191-200
    • Kennedy, A.R.1    Billings, P.C.2    Maki, P.A.3    Newberne, P.4
  • 39
    • 0028598821 scopus 로고
    • Field bean protease inhibitor preparations, unlike methotrexate, can completely suppress Yoshida sarcoma tumor in rats
    • Banerji A. P., Fernandes A. O., Field bean protease inhibitor preparations, unlike methotrexate, can completely suppress Yoshida sarcoma tumor in rats Cell Biology International 1994 18 11 1025 1034
    • (1994) Cell Biology International , vol.18 , Issue.11 , pp. 1025-1034
    • Banerji, A.P.1    Fernandes, A.O.2
  • 40
    • 0029117555 scopus 로고
    • Inhibition of benzopyrene-induced forestomach tumors by field bean protease inhibitor(s)
    • Fernandes A. O., Banerji A. P., Inhibition of benzopyrene-induced forestomach tumors by field bean protease inhibitor(s) Carcinogenesis 1995 16 8 1843 1846
    • (1995) Carcinogenesis , vol.16 , Issue.8 , pp. 1843-1846
    • Fernandes, A.O.1    Banerji, A.P.2
  • 41
    • 0030322705 scopus 로고    scopus 로고
    • Protein proteinase inhibitors in legume seedsoverview
    • Birk Y., Protein proteinase inhibitors in legume seedsoverview Archivos Latinoamericanos de Nutricin 1996 44 4, supplement 1 26S 30S
    • (1996) Archivos Latinoamericanos de Nutricin , vol.44 , Issue.4 SUPPL. 1
    • Birk, Y.1
  • 42
    • 0029815175 scopus 로고    scopus 로고
    • Erratum: The field bean protease inhibitor can effectively suppress 72-dimethylbenz[a]anthracene-induced skin tumorigenesis in mice
    • Fernandes A. O., Banerji A. P., Erratum: the field bean protease inhibitor can effectively suppress 72-dimethylbenz[a]anthracene-induced skin tumorigenesis in mice Cancer Letters 1996 106 1 145
    • (1996) Cancer Letters , vol.106 , Issue.1 , pp. 145
    • Fernandes, A.O.1    Banerji, A.P.2
  • 43
    • 0032479554 scopus 로고    scopus 로고
    • The field bean protease inhibitor has the potential to suppress B16F10 melanoma cell lung metastasis in mice
    • Banerji A., Fernandes A., Bane S., Ahire S., The field bean protease inhibitor has the potential to suppress B16F10 melanoma cell lung metastasis in mice Cancer Letters 1998 129 1 15 20
    • (1998) Cancer Letters , vol.129 , Issue.1 , pp. 15-20
    • Banerji, A.1    Fernandes, A.2    Bane, S.3    Ahire, S.4
  • 44
    • 0032147214 scopus 로고    scopus 로고
    • Protease inhibitors and carcinoma of the esophagus
    • Sammon A. M., Protease inhibitors and carcinoma of the esophagus Cancer 1998 83 3 405 408
    • (1998) Cancer , vol.83 , Issue.3 , pp. 405-408
    • Sammon, A.M.1
  • 45
    • 2942708160 scopus 로고    scopus 로고
    • A soybean Kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation
    • Kobayashi H., Suzuki M., Kanayama N., Terao T., A soybean Kunitz trypsin inhibitor suppresses ovarian cancer cell invasion by blocking urokinase upregulation Clinical and Experimental Metastasis 2004 21 2 159 166
    • (2004) Clinical and Experimental Metastasis , vol.21 , Issue.2 , pp. 159-166
    • Kobayashi, H.1    Suzuki, M.2    Kanayama, N.3    Terao, T.4
  • 46
    • 0015853344 scopus 로고
    • Maturation of the head of bacteriophage T4. I. DNA packaging events
    • Laemmli U. K., Favre M., Maturation of the head of bacteriophage T4. I. DNA packaging events Journal of Molecular Biology 1973 80 4 575 599
    • (1973) Journal of Molecular Biology , vol.80 , Issue.4 , pp. 575-599
    • Laemmli, U.K.1    Favre, M.2
  • 49
    • 0141518452 scopus 로고    scopus 로고
    • Gymnin, a potent defensin-like antifungal peptide from the Yunnan bean (Gymnocladus chinensis Baill)
    • Wong J. H., Ng T. B., Gymnin, a potent defensin-like antifungal peptide from the Yunnan bean (Gymnocladus chinensis Baill) Peptides 2003 24 7 963 968
    • (2003) Peptides , vol.24 , Issue.7 , pp. 963-968
    • Wong, J.H.1    Ng, T.B.2
  • 50
    • 0035824466 scopus 로고    scopus 로고
    • Pleureryn, a novel protease from fresh fruiting bodies of the edible mushroom Pleurotus eryngii
    • Wang H., Ng T. B., Pleureryn, a novel protease from fresh fruiting bodies of the edible mushroom Pleurotus eryngii Biochemical and Biophysical Research Communications 2001 289 3 750 755
    • (2001) Biochemical and Biophysical Research Communications , vol.289 , Issue.3 , pp. 750-755
    • Wang, H.1    Ng, T.B.2
  • 51
    • 0035937399 scopus 로고    scopus 로고
    • Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies
    • Wang H., Ng T. B., Isolation and characterization of velutin, a novel low-molecular-weight ribosome-inactivating protein from winter mushroom (Flammulina velutipes) fruiting bodies Life Sciences 2001 68 18 2151 2158
    • (2001) Life Sciences , vol.68 , Issue.18 , pp. 2151-2158
    • Wang, H.1    Ng, T.B.2
  • 52
    • 40749144830 scopus 로고    scopus 로고
    • Concurrent purification of two defense proteins from French bean seeds: A defensin-like antifungal peptide and a hemagglutinin
    • Leung E. H. W., Wong J. H., Ng T. B., Concurrent purification of two defense proteins from French bean seeds: a defensin-like antifungal peptide and a hemagglutinin Journal of Peptide Science 2008 14 3 349 353
    • (2008) Journal of Peptide Science , vol.14 , Issue.3 , pp. 349-353
    • Leung, E.H.W.1    Wong, J.H.2    Ng, T.B.3
  • 53
    • 0141741475 scopus 로고    scopus 로고
    • Isolation of cucurmoschin, a novel antifungal peptide abundant in arginine, glutamate and glycine residues from black pumpkin seeds
    • Wang H. X., Ng T. B., Isolation of cucurmoschin, a novel antifungal peptide abundant in arginine, glutamate and glycine residues from black pumpkin seeds Peptides 2003 24 7 969 972
    • (2003) Peptides , vol.24 , Issue.7 , pp. 969-972
    • Wang, H.X.1    Ng, T.B.2
  • 54
    • 0032516679 scopus 로고    scopus 로고
    • Treatment with field bean protease inhibitor can effectively repress ethylnitrosourea (ENU)-induced neoplasms of the nervous system in Sprague-Dawley rats
    • Banerji A., Fernandes A., Bane S., Treatment with field bean protease inhibitor can effectively repress ethylnitrosourea (ENU)-induced neoplasms of the nervous system in Sprague-Dawley rats Cancer Letters 1998 130 1-2 161 167
    • (1998) Cancer Letters , vol.130 , Issue.12 , pp. 161-167
    • Banerji, A.1    Fernandes, A.2    Bane, S.3
  • 56
    • 0036927831 scopus 로고    scopus 로고
    • A new peptidic protease inhibitor from Vicia faba seeds exhibits antifungal, HIV-1 reverse transcriptase inhibiting and mitogenic activities
    • Ye X. Y., Ng T. B., A new peptidic protease inhibitor from Vicia faba seeds exhibits antifungal, HIV-1 reverse transcriptase inhibiting and mitogenic activities Journal of Peptide Science 2002 8 12 656 662
    • (2002) Journal of Peptide Science , vol.8 , Issue.12 , pp. 656-662
    • Ye, X.Y.1    Ng, T.B.2
  • 57
    • 35549006732 scopus 로고    scopus 로고
    • Isolation and characterization of a trypsin-chymotrypsin inhibitor from the seeds of green lentil (Lens culinaris)
    • Cheung A. H. K., Ng T. B., Isolation and characterization of a trypsin-chymotrypsin inhibitor from the seeds of green lentil (Lens culinaris) Protein and Peptide Letters 2007 14 9 859 864
    • (2007) Protein and Peptide Letters , vol.14 , Issue.9 , pp. 859-864
    • Cheung, A.H.K.1    Ng, T.B.2
  • 58
    • 63449097272 scopus 로고    scopus 로고
    • Trypsin-chymotrypsin inhibitors from Vigna mungo seeds
    • Cheung A. H. K., Wong J. H., Ng T. B., Trypsin-chymotrypsin inhibitors from Vigna mungo seeds Protein and Peptide Letters 2009 16 3 277 284
    • (2009) Protein and Peptide Letters , vol.16 , Issue.3 , pp. 277-284
    • Cheung, A.H.K.1    Wong, J.H.2    Ng, T.B.3
  • 59
    • 1942516818 scopus 로고    scopus 로고
    • Multiple trypsin inhibitors from Momordica cochinchinensis seeds, the Chinese drug mubiezhi
    • Wong R. C. H., Fong W. P., Ng T. B., Multiple trypsin inhibitors from Momordica cochinchinensis seeds, the Chinese drug mubiezhi Peptides 2004 25 2 163 169
    • (2004) Peptides , vol.25 , Issue.2 , pp. 163-169
    • Wong, R.C.H.1    Fong, W.P.2    Ng, T.B.3
  • 60
    • 0017245824 scopus 로고
    • Trypsin isoinhibitors from garden beans (Phaseolus vulgaris)
    • Birk Y., Trypsin isoinhibitors from garden beans (Phaseolus vulgaris) Methods in Enzymology 1976 45 710 716
    • (1976) Methods in Enzymology , vol.45 , pp. 710-716
    • Birk, Y.1
  • 63
    • 0029761298 scopus 로고    scopus 로고
    • Amino acid sequence of the Phaseolus vulgaris var. Fogo na Serra inhibitor and interactive surface modeling for the enzyme-inhibitor complex
    • De Carvalho P. G. B., Bloch C. Jr., Morhy L., Da Silva M. C. M., De Mello L. V., Neshich G., Amino acid sequence of the Phaseolus vulgaris var. Fogo na Serra inhibitor and interactive surface modeling for the enzyme-inhibitor complex Journal of Protein Chemistry 1996 15 6 591 598
    • (1996) Journal of Protein Chemistry , vol.15 , Issue.6 , pp. 591-598
    • De Carvalho, P.G.B.1    Bloch Jr., C.2    Morhy, L.3    Da Silva, M.C.M.4    De Mello, L.V.5    Neshich, G.6
  • 64
    • 0029737141 scopus 로고    scopus 로고
    • Complete sequence, subunit structure, and complexes with pancreatic -amylase of an -amylase inhibitor from Phaseolus vulgaris white kidney beans
    • Kasahara K., Hayashi K., Arakawa T., Philo J. S., Wen J., Hara S., Yamaguchi H., Complete sequence, subunit structure, and complexes with pancreatic -amylase of an -amylase inhibitor from Phaseolus vulgaris white kidney beans Journal of Biochemistry 1996 120 1 177 183
    • (1996) Journal of Biochemistry , vol.120 , Issue.1 , pp. 177-183
    • Kasahara, K.1    Hayashi, K.2    Arakawa, T.3    Philo, J.S.4    Wen, J.5    Hara, S.6    Yamaguchi, H.7
  • 65
    • 0025166667 scopus 로고
    • Purification and characterization of an extracellular prolyl endopeptidase from Agaricus bisporus
    • Sattar A. K. M. A., Yamamoto N., Yoshimoto T., Tsuru D., Purification and characterization of an extracellular prolyl endopeptidase from Agaricus bisporus Journal of Biochemistry 1990 107 2 256 261
    • (1990) Journal of Biochemistry , vol.107 , Issue.2 , pp. 256-261
    • Sattar, A.K.M.A.1    Yamamoto, N.2    Yoshimoto, T.3    Tsuru, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.