메뉴 건너뛰기




Volumn 128, Issue 2, 1997, Pages 151-158

Dehydroascorbate reductase and monodehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein

Author keywords

Dehydroascorbate; DHA reductase; Ipomoea batatas (L.) Lam; MDA reductase; Monodehydroascorbate; Trypsin inhibitor

Indexed keywords

DEHYDROASCORBIC ACID REDUCTASE; MONOHYDROASCORBATE REDUCTASE; OXIDOREDUCTASE; TRYPSIN INHIBITOR; UNCLASSIFIED DRUG;

EID: 0030755059     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(97)00153-2     Document Type: Article
Times cited : (59)

References (38)
  • 1
    • 0030788093 scopus 로고    scopus 로고
    • Polyamine-bound trypsin inhibitors in sweet potato (Ipomoea batatas [L.] Lam cv. Tainong 57) storage roots, sprouted roots and sprouts
    • W.C. Hou, Y.H. Lin, Polyamine-bound trypsin inhibitors in sweet potato (Ipomoea batatas [L.] Lam cv. Tainong 57) storage roots, sprouted roots and sprouts, Plant Sci. 126 (1997) 11-19.
    • (1997) Plant Sci. , vol.126 , pp. 11-19
    • Hou, W.C.1    Lin, Y.H.2
  • 2
    • 0001329109 scopus 로고
    • Proteolytic enzymes and their inhibitors in plants
    • C.A. Ryan, Proteolytic enzymes and their inhibitors in plants, Annu. Rev. Plant Physiol. 24 (1973) 173-196.
    • (1973) Annu. Rev. Plant Physiol. , vol.24 , pp. 173-196
    • Ryan, C.A.1
  • 3
    • 0024570553 scopus 로고
    • Protease inhibitor gene families: Strategies for transformation to improve plant defenses against herbivores
    • C.A. Ryan, Protease inhibitor gene families: strategies for transformation to improve plant defenses against herbivores, BioEssays 10 (1989) 20-24.
    • (1989) BioEssays , vol.10 , pp. 20-24
    • Ryan, C.A.1
  • 4
    • 0000487837 scopus 로고
    • Trypsin inhibitors in Indian foodstuffs: I Inhibitors in vegetables
    • K. Sohonie, A.P. Bhandarker, Trypsin inhibitors in Indian foodstuffs: I Inhibitors in vegetables, J. Sci. Ind. Res. 13B (1954) 500-503.
    • (1954) J. Sci. Ind. Res. , vol.13 B , pp. 500-503
    • Sohonie, K.1    Bhandarker, A.P.2
  • 5
    • 0002165231 scopus 로고
    • Level and heat stability of trypsin inhibitor activity among sweet potato (Ipomoea batatas Lam.) varieties
    • Y.H. Lin, H.L. Chen, Level and heat stability of trypsin inhibitor activity among sweet potato (Ipomoea batatas Lam.) varieties, Bot. Bull. Acad. Sin. 21 (1980) 1-13.
    • (1980) Bot. Bull. Acad. Sin. , vol.21 , pp. 1-13
    • Lin, Y.H.1    Chen, H.L.2
  • 6
    • 0000919249 scopus 로고
    • Relationship between trypsin-inhibitor activity and water-soluble protein and cumulative rainfall in sweet potatoes
    • Y.H. Lin, Relationship between trypsin-inhibitor activity and water-soluble protein and cumulative rainfall in sweet potatoes, J. Amer. Soc. Hort. Sci. 114 (1989) 814-818.
    • (1989) J. Amer. Soc. Hort. Sci. , vol.114 , pp. 814-818
    • Lin, Y.H.1
  • 7
    • 0343072156 scopus 로고
    • Increasing or inducing trypsin inhibitor biosynthesis of sweet potato stem culture by heating or with 6-benzylaminopurine
    • held at Shanghai, Nov. 16-21
    • P.J. Tsai, Y.H. Lin, Increasing or inducing trypsin inhibitor biosynthesis of sweet potato stem culture by heating or with 6-benzylaminopurine, (abstract) 6th Federation of Asian and Oceanian Biochemists Congress, held at Shanghai, Nov. 16-21, 1992, p. 223.
    • (1992) 6th Federation of Asian and Oceanian Biochemists Congress , pp. 223
    • Tsai, P.J.1    Lin, Y.H.2
  • 9
    • 0000445548 scopus 로고
    • Characterization of major proteins in sweet potato tuberous roots
    • M. Maeshima, T. Sasaki, T. Asahi, Characterization of major proteins in sweet potato tuberous roots, Phytochemistry 24 (1985) 1899-1902.
    • (1985) Phytochemistry , vol.24 , pp. 1899-1902
    • Maeshima, M.1    Sasaki, T.2    Asahi, T.3
  • 10
    • 0343072155 scopus 로고
    • Biochemical and histological studies of trypsin inhibitors of sweet potato (Ipomoea batatas (L.) Lam.)
    • Y.H. Wei, K.F. Chak (Eds.), Taipei
    • Y.H. Lin, Biochemical and histological studies of trypsin inhibitors of sweet potato (Ipomoea batatas (L.) Lam.), in: Y.H. Wei, K.F. Chak (Eds.), Advances in Biotechnology and Molecular Biology, National Science Council Monograph Series No. 15, Taipei, 1990, pp. 115-130.
    • (1990) Advances in Biotechnology and Molecular Biology, National Science Council Monograph Series , vol.15 , pp. 115-130
    • Lin, Y.H.1
  • 11
    • 0001212544 scopus 로고
    • Trypsin inhibitors of sweet potato: Review and prospect
    • Y.I. Hsing, C.H. Chou (Eds.), Taipei
    • Y.H. Lin, Trypsin inhibitors of sweet potato: review and prospect, in: Y.I. Hsing, C.H. Chou (Eds.), Recent Advances in Botany, Academia Sinica Monograph Series No. 13, Taipei, 1993, pp. 179-185.
    • (1993) Recent Advances in Botany, Academia Sinica Monograph Series , vol.13 , pp. 179-185
    • Lin, Y.H.1
  • 12
    • 0002432259 scopus 로고    scopus 로고
    • Cultivar differences in trypsin inhibitory activities of sweet potato leaves and tuberous roots
    • H.Y. Wang, K.W. Yeh, Cultivar differences in trypsin inhibitory activities of sweet potato leaves and tuberous roots, Taiwania 41 (1996) 27-34.
    • (1996) Taiwania , vol.41 , pp. 27-34
    • Wang, H.Y.1    Yeh, K.W.2
  • 13
    • 0024287753 scopus 로고
    • Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector
    • D.L. Andrews, B. Beames, M.D. Summers, W.D. Park, Characterization of the lipid acyl hydrolase activity of the major potato (Solanum tuberosum) tuber protein, patatin, by cloning and abundant expression in a baculovirus vector, Biochem. J. 252 (1988) 199-206.
    • (1988) Biochem. J. , vol.252 , pp. 199-206
    • Andrews, D.L.1    Beames, B.2    Summers, M.D.3    Park, W.D.4
  • 14
    • 0026650480 scopus 로고
    • The soybean vegetative storage proteins VSP α and VSP β are acid phosphatases active on polyphosphates
    • D.B. Dewald, H.S. Mason, J.E. Mullet, The soybean vegetative storage proteins VSP α and VSP β are acid phosphatases active on polyphosphates, J. Biol. Chem. 267 (1992) 15958-15964.
    • (1992) J. Biol. Chem. , vol.267 , pp. 15958-15964
    • Dewald, D.B.1    Mason, H.S.2    Mullet, J.E.3
  • 15
    • 0028136613 scopus 로고
    • A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
    • S. Trümper, H. Follmann, I. Häberlein, A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor, FEBS Lett. 352 (1994) 159-162.
    • (1994) FEBS Lett. , vol.352 , pp. 159-162
    • Trümper, S.1    Follmann, H.2    Häberlein, I.3
  • 16
    • 0000746853 scopus 로고
    • Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules
    • D.A. Dalton, S.A. Russell, F.J. Hanus, G.A. Pascoe, H.J. Evans, Enzymatic reactions of ascorbate and glutathione that prevent peroxide damage in soybean root nodules, Proc. Natl. Acad. Sci. USA 83 (1986) 3811-3815.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3811-3815
    • Dalton, D.A.1    Russell, S.A.2    Hanus, F.J.3    Pascoe, G.A.4    Evans, H.J.5
  • 17
    • 0028825699 scopus 로고
    • A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis
    • K. Kobayashi, S. Tagawa, S. Sano, K. Asada, A direct demonstration of the catalytic action of monodehydroascorbate reductase by pulse radiolysis, J. Biol. Chem. 270 (1995) 27551-27554.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27551-27554
    • Kobayashi, K.1    Tagawa, S.2    Sano, S.3    Asada, K.4
  • 18
    • 0027460271 scopus 로고
    • Antioxidant role of dehydroascorbic acid reductase in insects
    • C.B. Summers, G.W. Felton, Antioxidant role of dehydroascorbic acid reductase in insects, Biochim. Biophys. Acta. 1156 (1993) 235-238.
    • (1993) Biochim. Biophys. Acta. , vol.1156 , pp. 235-238
    • Summers, C.B.1    Felton, G.W.2
  • 19
    • 77957181306 scopus 로고
    • Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids
    • C. Miyake, K. Asada, Thylakoid-bound ascorbate peroxidase in spinach chloroplasts and photoreduction of its primary oxidation product monodehydroascorbate radicals in thylakoids, Plant Cell Physiol. 33 (1992) 541-553.
    • (1992) Plant Cell Physiol. , vol.33 , pp. 541-553
    • Miyake, C.1    Asada, K.2
  • 20
    • 84983392009 scopus 로고
    • Ascorbate peroxidase - A hydrogen peroxide scavenging enzyme in chloroplasts
    • K. Asada, Ascorbate peroxidase - a hydrogen peroxide scavenging enzyme in chloroplasts, Physiol. Plant 85 (1992) 235-241.
    • (1992) Physiol. Plant , vol.85 , pp. 235-241
    • Asada, K.1
  • 22
    • 0029189399 scopus 로고
    • A specific ascorbate free radical reductase isozyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria
    • S. De Leonardis, G. De Lorenzo, G. Borraccino, S. Dipierro, A specific ascorbate free radical reductase isozyme participates in the regeneration of ascorbate for scavenging toxic oxygen species in potato tuber mitochondria, Plant Physiol. 109 (1995) 847-851.
    • (1995) Plant Physiol. , vol.109 , pp. 847-851
    • De Leonardis, S.1    De Lorenzo, G.2    Borraccino, G.3    Dipierro, S.4
  • 23
    • 0242492488 scopus 로고
    • Subcellular location of redox enzymes involving ascorbic acid in cucumber fruit
    • N. Yamuchi, K. Yamawaki, Y. Ueda, K. Chachin, Subcellular location of redox enzymes involving ascorbic acid in cucumber fruit, J. Jpn. Soc. Hort. Sci. 53 (1984) 347-353.
    • (1984) J. Jpn. Soc. Hort. Sci. , vol.53 , pp. 347-353
    • Yamuchi, N.1    Yamawaki, K.2    Ueda, Y.3    Chachin, K.4
  • 24
    • 0000594637 scopus 로고
    • Purification and properties of ascorbate free-radical reductase from potato tubers
    • G. Borraccino, S. Dipierro, O. Arrigoni, Purification and properties of ascorbate free-radical reductase from potato tubers, Planta 167 (1986) 521-526.
    • (1986) Planta , vol.167 , pp. 521-526
    • Borraccino, G.1    Dipierro, S.2    Arrigoni, O.3
  • 25
    • 0002668438 scopus 로고
    • Soluble ascorbate peroxidase from potato tubers
    • M.R. Elia, G. Borraccino, S. Dipierro, Soluble ascorbate peroxidase from potato tubers, Plant Sci. 85 (1992) 17-21.
    • (1992) Plant Sci. , vol.85 , pp. 17-21
    • Elia, M.R.1    Borraccino, G.2    Dipierro, S.3
  • 26
    • 0000918942 scopus 로고
    • Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide
    • M.A. Hossain, Y. Nakano, K. Asada, Monodehydroascorbate reductase in spinach chloroplasts and its participation in regeneration of ascorbate for scavenging hydrogen peroxide, Plant Cell Physiol. 25 (1984) 385-395.
    • (1984) Plant Cell Physiol. , vol.25 , pp. 385-395
    • Hossain, M.A.1    Nakano, Y.2    Asada, K.3
  • 27
    • 0030425635 scopus 로고    scopus 로고
    • Monodehydroascorbate radical detected by electron para-magnetic resonance spectrometry is a sensitive probe of oxidative stress in intact leaves
    • U. Heber, C. Miyake, J. Mano, C. Ohno, K. Asada, Monodehydroascorbate radical detected by electron para-magnetic resonance spectrometry is a sensitive probe of oxidative stress in intact leaves, Plant Cell Physiol. 37 (1996) 1066-1072.
    • (1996) Plant Cell Physiol. , vol.37 , pp. 1066-1072
    • Heber, U.1    Miyake, C.2    Mano, J.3    Ohno, C.4    Asada, K.5
  • 28
    • 0029111330 scopus 로고
    • Trypsin inhibitor and trypsin-like protease activity in air- or submergence- grown rice (Oryza sativa L.) coleoptiles
    • T.M. Lee, Y.H. Lin, Trypsin inhibitor and trypsin-like protease activity in air- or submergence- grown rice (Oryza sativa L.) coleoptiles, Plant Sci. 106 (1995) 43-54.
    • (1995) Plant Sci. , vol.106 , pp. 43-54
    • Lee, T.M.1    Lin, Y.H.2
  • 30
    • 0002977651 scopus 로고
    • Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions
    • I. Yamazaki, L.H. Pette, Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions, Biochem. Biophys. Acta. 50 (1961) 62-69.
    • (1961) Biochem. Biophys. Acta. , vol.50 , pp. 62-69
    • Yamazaki, I.1    Pette, L.H.2
  • 31
    • 0001277128 scopus 로고
    • Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia
    • J.C. Kaplan, E. Beutler, Electrophoresis of red cell NADH- and NADPH-diaphorases in normal subjects and patients with congenital methemoglobinemia, Biochem. Biophys. Res. Commun. 29 (1967) 605-610.
    • (1967) Biochem. Biophys. Res. Commun. , vol.29 , pp. 605-610
    • Kaplan, J.C.1    Beutler, E.2
  • 32
    • 0025082330 scopus 로고
    • Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity
    • W.W. Wells, D.P. Wu, Y. Yang, P.A. Rocque, Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity, J. Biol. Chem. 265 (1990) 15361-15364.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15361-15364
    • Wells, W.W.1    Wu, D.P.2    Yang, Y.3    Rocque, P.A.4
  • 33
    • 0029294031 scopus 로고
    • Subunit interaction enhances enzyme activity and stability of sweet potato cytosolic Cu/Zn-superoxide dismutase purified by a His-tagged recombinant protein method
    • C.T. Lin, M.T. Lin, Y.T. Chen, J.F. Shaw, Subunit interaction enhances enzyme activity and stability of sweet potato cytosolic Cu/Zn-superoxide dismutase purified by a His-tagged recombinant protein method, Plant Mol. Biol. 28 (1995) 303-311.
    • (1995) Plant Mol. Biol. , vol.28 , pp. 303-311
    • Lin, C.T.1    Lin, M.T.2    Chen, Y.T.3    Shaw, J.F.4
  • 34
    • 0021309470 scopus 로고
    • Determination of microbial damage caused by oxygen free radicals, and the protective role of superoxide dismutase
    • H.M. Hassan, Determination of microbial damage caused by oxygen free radicals, and the protective role of superoxide dismutase, Meth. Enzymol. 105 (1984) 405-412.
    • (1984) Meth. Enzymol. , vol.105 , pp. 405-412
    • Hassan, H.M.1
  • 36
    • 0025944354 scopus 로고
    • Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins
    • K. Kobrehel, B.C. Yee, B.B. Buchanan, Role of the NADP/thioredoxin system in the reduction of α-amylase and trypsin inhibitor proteins, J. Biol. Chem. 266 (1991) 16135-16140.
    • (1991) J. Biol. Chem. , vol.266 , pp. 16135-16140
    • Kobrehel, K.1    Yee, B.C.2    Buchanan, B.B.3
  • 37
    • 38249025545 scopus 로고
    • Interaction of ascorbate free radical reductase with sulphhydryl reagents
    • G. Borraccino, S. Dipierro, O. Arrigoni, Interaction of ascorbate free radical reductase with sulphhydryl reagents, Phytochemistry 28 (1989) 715-717.
    • (1989) Phytochemistry , vol.28 , pp. 715-717
    • Borraccino, G.1    Dipierro, S.2    Arrigoni, O.3
  • 38
    • 0026497715 scopus 로고
    • Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cell
    • M.R. Fernando, H. Nanri, S. Yoshitake, K. Nagata-Kuno, S. Minakami, Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cell, Eur. J. Biochem. 209 (1992) 917-922.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 917-922
    • Fernando, M.R.1    Nanri, H.2    Yoshitake, S.3    Nagata-Kuno, K.4    Minakami, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.