메뉴 건너뛰기




Volumn 163, Issue 4, 2002, Pages 733-739

Sweet potato (Ipomoea batatas (L.) Lam) trypsin inhibitors, the major root storage proteins, inhibit one endogenous serine protease activity

Author keywords

Physiological function; Regulation; Serine protease; Sweet potato; Trypsin inhibitor

Indexed keywords

DEGRADATION; ENZYME INHIBITION; PHYSIOLOGY; PROTEINS;

EID: 0036804578     PISSN: 01689452     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9452(02)00168-1     Document Type: Article
Times cited : (14)

References (36)
  • 1
    • 0020410219 scopus 로고
    • Comparative biochemistry of the proteinases of eukaryotic microorganism
    • M.J. North, Comparative biochemistry of the proteinases of eukaryotic microorganism, Microbiol. Rev. 46 (1982) 308-340.
    • (1982) Microbiol. Rev. , vol.46 , pp. 308-340
    • North, M.J.1
  • 2
    • 0001743127 scopus 로고
    • Control of storage protein metabolism in the cotyledons of germinating mung beans: Role of endopeptidase
    • M.J. Chrispeels, D. Boulter, Control of storage protein metabolism in the cotyledons of germinating mung beans: Role of endopeptidase, Plant Physiol. 55 (1975) 1031-1037.
    • (1975) Plant Physiol. , vol.55 , pp. 1031-1037
    • Chrispeels, M.J.1    Boulter, D.2
  • 3
    • 0002581206 scopus 로고
    • Differential proteolysis of glycinin and β-conglycinin polypeptides during soybean germination and seedling growth
    • K.A. Wilson, B.R. Rightmire, J.C. Chen, A.L. Tan-Wilson, Differential proteolysis of glycinin and β-conglycinin polypeptides during soybean germination and seedling growth, Plant Physiol. 82 (1986) 71-76.
    • (1986) Plant Physiol. , vol.82 , pp. 71-76
    • Wilson, K.A.1    Rightmire, B.R.2    Chen, J.C.3    Tan-Wilson, A.L.4
  • 4
    • 0001098671 scopus 로고
    • Characterization of the major protease involved in the soybean β-conglycinin storage protein mobilization
    • X. Qi, K.A. Wilson, A.L. Tan-Wilson, Characterization of the major protease involved in the soybean β-conglycinin storage protein mobilization, Plant Physiol. 99 (1992) 725-733.
    • (1992) Plant Physiol. , vol.99 , pp. 725-733
    • Qi, X.1    Wilson, K.A.2    Tan-Wilson, A.L.3
  • 5
  • 6
    • 0032401579 scopus 로고    scopus 로고
    • Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings?
    • V. Senyuk, V. Rotari, C. Becker, A. Zakharov, C. Horstmann, K. Muntz, I. Vaimtraub, Does an asparaginyl-specific cysteine endopeptidase trigger phaseolin degradation in cotyledons of kidney bean seedlings?, Eur. J. Biochem. 258 (1998) 546-558.
    • (1998) Eur. J. Biochem. , vol.258 , pp. 546-558
    • Senyuk, V.1    Rotari, V.2    Becker, C.3    Zakharov, A.4    Horstmann, C.5    Muntz, K.6    Vaimtraub, I.7
  • 8
    • 0002894028 scopus 로고
    • In vitro protease activities of four parts of germinated Tainong 57 sweet potato roots
    • Y.H. Lin, M. Tsai, In vitro protease activities of four parts of germinated Tainong 57 sweet potato roots, Bot. Bull. Acad. Sin. 32 (1991) 79-85.
    • (1991) Bot. Bull. Acad. Sin. , vol.32 , pp. 79-85
    • Lin, Y.H.1    Tsai, M.2
  • 9
    • 0000222928 scopus 로고
    • An aminopeptidase (APl) from sprouts of sweet potato (Ipomoea batatas L. Lam cv. Tainong 64)
    • Y.H. Lin, H.Y. Chan, An aminopeptidase (APl) from sprouts of sweet potato (Ipomoea batatas L. Lam cv. Tainong 64), Bot. Bull. Acad. Sin. 33 (1992) 253-261.
    • (1992) Bot. Bull. Acad. Sin. , vol.33 , pp. 253-261
    • Lin, Y.H.1    Chan, H.Y.2
  • 10
    • 0028094134 scopus 로고
    • Purification and characterization of an enzyme hydrolyzing L-methionine-4-nitroanilide from germinated sweet potato (Ipomoea batatas L. Lam cv. Tainong 57) root
    • Y.H. Lin, M. Tsai, Purification and characterization of an enzyme hydrolyzing L-methionine-4-nitroanilide from germinated sweet potato (Ipomoea batatas L. Lam cv. Tainong 57) root, Bot. Bull. Acad. Sin. 35 (1994) 25-32.
    • (1994) Bot. Bull. Acad. Sin. , vol.35 , pp. 25-32
    • Lin, Y.H.1    Tsai, M.2
  • 11
    • 0029770224 scopus 로고    scopus 로고
    • Characterization of the endoprotease appearing during wheat grain development
    • F. Dominguez, F.J. Cejudo, Characterization of the endoprotease appearing during wheat grain development, Plant Physiol. 112 (1996) 1211-1217.
    • (1996) Plant Physiol. , vol.112 , pp. 1211-1217
    • Dominguez, F.1    Cejudo, F.J.2
  • 12
    • 0027597690 scopus 로고
    • Developmental and age-related processes that inference the longevity and senescence of photosynthetic tissues in Arabidopsis
    • L.L. Hensel, V. Grbic, D.A. Baumgarten, A.B. Bleecker, Developmental and age-related processes that inference the longevity and senescence of photosynthetic tissues in Arabidopsis, Plant Cell 5 (1993) 553-564.
    • (1993) Plant Cell , vol.5 , pp. 553-564
    • Hensel, L.L.1    Grbic, V.2    Baumgarten, D.A.3    Bleecker, A.B.4
  • 13
    • 0028134248 scopus 로고
    • Molecular analysis of natural leaf senescence in Arabidopsis thalian
    • K.N. Lohman, G. Susheng, C.J. Manorama, R.M. Amasino, Molecular analysis of natural leaf senescence in Arabidopsis thalian, Physiol. Plant. 92 (1994) 322-328.
    • (1994) Physiol. Plant. , vol.92 , pp. 322-328
    • Lohman, K.N.1    Susheng, G.2    Manorama, C.J.3    Amasino, R.M.4
  • 15
    • 0030087809 scopus 로고    scopus 로고
    • Isolation and analysis of cDNA encoding tomato cysteine proteases expressed during leaf senescence
    • R. Drake, I. John, A. Farrell, W. Copper, W. Schuch, D. Grierson, Isolation and analysis of cDNA encoding tomato cysteine proteases expressed during leaf senescence, Plant Mol. Biol. 30 (1996) 755-767.
    • (1996) Plant Mol. Biol. , vol.30 , pp. 755-767
    • Drake, R.1    John, I.2    Farrell, A.3    Copper, W.4    Schuch, W.5    Grierson, D.6
  • 16
    • 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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. Am. Soc. Hort. Sci. 114 (1989) 814-818.
    • (1989) J. Am. Soc. Hort. Sci. , vol.114 , pp. 814-818
    • Lin, Y.H.1
  • 21
    • 0030788093 scopus 로고    scopus 로고
    • Polyamine-bound trypsin inhibitors in sweet potato (Ipomoea batatas [L.] Lam cv. Tainong 570 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 570 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
  • 22
    • 0030755059 scopus 로고    scopus 로고
    • Dehydroascorbate reductase and mono-dehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein
    • W.C. Hou, H.Y. Lin, Dehydroascorbate reductase and mono-dehydroascorbate reductase activities of trypsin inhibitors, the major sweet potato (Ipomoea batatas [L.] Lam) root storage protein, Plant Sci. 128 (1997) 151-158.
    • (1997) Plant Sci. , vol.128 , pp. 151-158
    • Hou, W.C.1    Lin, H.Y.2
  • 23
    • 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
  • 24
    • 0001212544 scopus 로고
    • Trypsin inhibitors of sweet potato: Review and prospect
    • Y.I. Hsing, C.H. Chou (Eds.), Taipei, Taiwan
    • 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, Taiwan, 1993, pp. 179-185.
    • (1993) Recent Advances in Botany, Academia Sinica Monograph Series , vol.13 , pp. 179-185
    • Lin, Y.H.1
  • 25
    • 0031081795 scopus 로고    scopus 로고
    • Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): A tuber storage protein with trypsin inhibitory activity
    • K.W. Yeh, J.C. Chen, M.I. Lin, Y.M. Chen, C.Y. Lin, Functional activity of sporamin from sweet potato (Ipomoea batatas Lam.): A tuber storage protein with trypsin inhibitory activity, Plant Mol. Biol. 33 (1997) 565-570.
    • (1997) Plant Mol. Biol. , vol.33 , pp. 565-570
    • Yeh, K.W.1    Chen, J.C.2    Lin, M.I.3    Chen, Y.M.4    Lin, C.Y.5
  • 26
    • 0030750613 scopus 로고    scopus 로고
    • Sweet potato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura
    • K.W. Yeh, M.L. Lin, S.J. Tuan, Y.M. Chen, C.Y. Lin, S.S. Kao, Sweet potato (Ipomoea batatas) trypsin inhibitors expressed in transgenic tobacco plants confer resistance against Spodoptera litura, Plant Cell Rep. 16 (1997) 696-699.
    • (1997) Plant Cell Rep. , vol.16 , pp. 696-699
    • Yeh, K.W.1    Lin, M.L.2    Tuan, S.J.3    Chen, Y.M.4    Lin, C.Y.5    Kao, S.S.6
  • 28
    • 0022262821 scopus 로고
    • Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: A systematic analysis
    • V. Neuhoff, R. Stamm, H. Eibl, Clear background and highly sensitive protein staining with Coomassie blue dyes in polyacrylamide gels: A systematic analysis, Electrophoresis 6 (1985) 427-448.
    • (1985) Electrophoresis , vol.6 , pp. 427-448
    • Neuhoff, V.1    Stamm, R.2    Eibl, H.3
  • 29
    • 0031936391 scopus 로고    scopus 로고
    • Activity staining on polyacrylamide gels of trypsin inhibitors from leaves of sweet potato (Ipomoea batatas [L.] Lam) varieties
    • W.C. Hou, Y.H. Lin, Activity staining on polyacrylamide gels of trypsin inhibitors from leaves of sweet potato (Ipomoea batatas [L.] Lam) varieties, Electrophoresis 19 (1998) 212-214.
    • (1998) Electrophoresis , vol.19 , pp. 212-214
    • Hou, W.C.1    Lin, Y.H.2
  • 30
    • 0000092210 scopus 로고
    • Major soluble proteins of sweet potato roots and changes in proteins after cutting, infection, or storage
    • H.S. Li, K. Oba, Major soluble proteins of sweet potato roots and changes in proteins after cutting, infection, or storage, Agric. Biol. Chem. 49 (1985) 737-744.
    • (1985) Agric. Biol. Chem. , vol.49 , pp. 737-744
    • Li, H.S.1    Oba, K.2
  • 31
    • 0023229057 scopus 로고
    • A membrane-bound, calcium-dependent protease in yeast α-cell cleaving on the carboxyl side of paired basic residues
    • K. Mizuno, T. Nakamura, K. Takada, S. Sakakibara, H. Matsuo, A membrane-bound, calcium-dependent protease in yeast α-cell cleaving on the carboxyl side of paired basic residues, Biochem. Biophys. Res. Commun. 144 (1987) 807-814.
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 807-814
    • Mizuno, K.1    Nakamura, T.2    Takada, K.3    Sakakibara, S.4    Matsuo, H.5
  • 32
    • 0025858835 scopus 로고
    • A single-step separation of the one- and two-chain forms of tissue plasminogen activator
    • S.S. Husain, A single-step separation of the one- and two-chain forms of tissue plasminogen activator, Arch. Biochem. Biophys. 285 (1991) 373-376.
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 373-376
    • Husain, S.S.1
  • 33
    • 0028136613 scopus 로고
    • A novel dehydroascorbate reductase from spinach chloroplasts homologous to plant trypsin inhibitor
    • S. Trumper, H. Follmann, I. Haberlein, 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
    • Trumper, S.1    Follmann, H.2    Haberlein, I.3
  • 34
    • 0019886687 scopus 로고
    • Secondary structure of reduced ovomucoid and denaturation of reduced ovomucoid and its reduced fragment A (1-130) and B (131-186)
    • T. Matsuda, K. Watanabe, Y. Sato, Secondary structure of reduced ovomucoid and denaturation of reduced ovomucoid and its reduced fragment A (1-130) and B (131-186), FEBS Lett. 124 (1981) 185-188.
    • (1981) FEBS Lett. , vol.124 , pp. 185-188
    • Matsuda, T.1    Watanabe, K.2    Sato, Y.3
  • 35
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.