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Volumn 152, Issue 1, 1998, Pages 44-50

Effect of anoxia on gibberellic acid-induced protease and β-amylase processing in barley seeds

Author keywords

Anoxia; Barley; Endoprotease; Hordeum vulgare L; amylase

Indexed keywords


EID: 0031889287     PISSN: 01761617     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0176-1617(98)80100-4     Document Type: Article
Times cited : (9)

References (23)
  • 1
    • 84948497920 scopus 로고
    • Post-translational modification of β-amylases during germination of wheat and rye seeds
    • D. Bureau C. Lauriere C. Mayer J. Sadowsh J. Daussant Post-translational modification of β-amylases during germination of wheat and rye seeds J. Plant Physiol. 134 1989 678 684
    • (1989) J. Plant Physiol. , vol.134 , pp. 678-684
    • Bureau, D.1    Lauriere, C.2    Mayer, C.3    Sadowsh, J.4    Daussant, J.5
  • 2
    • 0000144655 scopus 로고
    • Cereal β-amyiase immunochemical study on two enzyme-deficient inbred lines of rye
    • J. Daussant B. Zbaszyniak J. Sadowski I. Wiatroszak Cereal β-amyiase immunochemical study on two enzyme-deficient inbred lines of rye Planta 151 1981 176 179
    • (1981) Planta , vol.151 , pp. 176-179
    • Daussant, J.1    Zbaszyniak, B.2    Sadowski, J.3    Wiatroszak, I.4
  • 3
    • 0001765463 scopus 로고
    • A model for starch breakdown in higher plants
    • G. Dunn A model for starch breakdown in higher plants Phytochemistry 13 1974 1341 1346
    • (1974) Phytochemistry , vol.13 , pp. 1341-1346
    • Dunn, G.1
  • 4
    • 0001599901 scopus 로고
    • Synthesis of salt-soluble proteins in barley. Pulse-labelling study of grain filling in liquid-cultured detached spikes
    • H. Giese J. Hejgaard Synthesis of salt-soluble proteins in barley. Pulse-labelling study of grain filling in liquid-cultured detached spikes Planta 161 1984 172 177
    • (1984) Planta , vol.161 , pp. 172-177
    • Giese, H.1    Hejgaard, J.2
  • 5
    • 0000274656 scopus 로고    scopus 로고
    • The release of bound beta-amylase by macromolecules
    • K.H. Grime D.E. Briggs The release of bound beta-amylase by macromolecules J. of the Institute of Brewing 102 1996 261 270
    • (1996) J. of the Institute of Brewing , vol.102 , pp. 261-270
    • Grime, K.H.1    Briggs, D.E.2
  • 6
    • 0001876687 scopus 로고
    • Release and activation of barleybeta-amylase by malt endopeptidases
    • J.R. Guerin R.C.M. Lance W. Wallace Release and activation of barley beta -amylase by malt endopeptidases J. Cer. Sci. 15 1992 5 14
    • (1992) J. Cer. Sci. , vol.15 , pp. 5-14
    • Guerin, J.R.1    Lance, R.C.M.2    Wallace, W.3
  • 7
    • 0029201279 scopus 로고
    • Amylolytic activities in cereal seeds under aerobic and anaerobic conditions
    • L. Guglielminetti J. Yamaguchi P. Perata A. Alpi Amylolytic activities in cereal seeds under aerobic and anaerobic conditions Plant Physiol. 109 1995 1069 1076
    • (1995) Plant Physiol. , vol.109 , pp. 1069-1076
    • Guglielminetti, L.1    Yamaguchi, J.2    Perata, P.3    Alpi, A.4
  • 8
    • 0028878441 scopus 로고
    • Effect of anoxia on carbohydrate metabolism in rice seedlings
    • L. Guglielminetti P. Perata A. Alpi Effect of anoxia on carbohydrate metabolism in rice seedlings Plant Physiol. 108 1995 735 741
    • (1995) Plant Physiol. , vol.108 , pp. 735-741
    • Guglielminetti, L.1    Perata, P.2    Alpi, A.3
  • 9
    • 0001992521 scopus 로고
    • Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers
    • P.W. Hammerton T.-H.D. Ho Hormonal regulation of the development of protease and carboxypeptidase activities in barley aleurone layers Plant Physiol. 80 1986 692 697
    • (1986) Plant Physiol. , vol.80 , pp. 692-697
    • Hammerton, P.W.1    Ho, T.-H.D.2
  • 10
    • 0000992348 scopus 로고
    • Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during desiccation phase of seed development
    • I. Hara-Nishimura M. Nishimura J. Daussant Conversion of free β-amylase to bound β-amylase on starch granules in the barley endosperm during desiccation phase of seed development Protoplasma 134 1986 149 153
    • (1986) Protoplasma , vol.134 , pp. 149-153
    • Hara-Nishimura, I.1    Nishimura, M.2    Daussant, J.3
  • 11
    • 84982694135 scopus 로고
    • Germination and seedling growth under aerobic conditions in Echinochloa crus-galli (barnyard grass)
    • P.A. Kennedy S.C.H. Barret D. van der Zee M.E. Rumpho Germination and seedling growth under aerobic conditions in Echinochloa crus-galli (barnyard grass) Plant Cell Environ. 3 1980 243 248
    • (1980) Plant Cell Environ. , vol.3 , pp. 243-248
    • Kennedy, P.A.1    Barret, S.C.H.2    van der Zee, D.3    Rumpho, M.E.4
  • 12
    • 0002898965 scopus 로고
    • Purification and characterization of gibberellic acid-induced cysteine endoproteases in barley aleurone layers
    • S.M. Koehler T.-H.D. Ho Purification and characterization of gibberellic acid-induced cysteine endoproteases in barley aleurone layers Plant Physiol. 87 1988 95 103
    • (1988) Plant Physiol. , vol.87 , pp. 95-103
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 13
    • 0000023298 scopus 로고
    • A major gibberellic acid-induced barley aleurone cysteine proteinase which digests hordein. Purification and characterization
    • S.M. Koehler T.-H.D. Ho A major gibberellic acid-induced barley aleurone cysteine proteinase which digests hordein. Purification and characterization Plant Physiol. 94 1990 251 258
    • (1990) Plant Physiol. , vol.94 , pp. 251-258
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 14
    • 0025465440 scopus 로고
    • Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers
    • S.M. Koehler T.-H.D. Ho Hormonal regulation, processing, and secretion of cysteine proteinases in barley aleurone layers The Plant Cell 2 1990 769 783
    • (1990) The Plant Cell , vol.2 , pp. 769-783
    • Koehler, S.M.1    Ho, T.-H.D.2
  • 16
    • 84913845038 scopus 로고
    • Immunohistochemical localization of beta-amylase in resting barley seeds
    • C. Lauriere M. Lauriere J. Daussant Immunohistochemical localization of beta-amylase in resting barley seeds Physiol. Plant. 67 1986 383 388
    • (1986) Physiol. Plant. , vol.67 , pp. 383-388
    • Lauriere, C.1    Lauriere, M.2    Daussant, J.3
  • 17
    • 0014606572 scopus 로고
    • Enzymes associated with protein bodies isolated from ungerminated barley seeds
    • P.L. Ory K.W. Henningsen Enzymes associated with protein bodies isolated from ungerminated barley seeds Plant Physiol. 44 1969 1488 1498
    • (1969) Plant Physiol. , vol.44 , pp. 1488-1498
    • Ory, P.L.1    Henningsen, K.W.2
  • 18
    • 0000073814 scopus 로고
    • Effect of anoxia on starch breakdown in rice and wheat seeds
    • P. Perata J. Pozueta-Romero T. Akazawa J. Yamaguchi Effect of anoxia on starch breakdown in rice and wheat seeds Planta 188 1992 611 618
    • (1992) Planta , vol.188 , pp. 611-618
    • Perata, P.1    Pozueta-Romero, J.2    Akazawa, T.3    Yamaguchi, J.4
  • 19
    • 0000833650 scopus 로고
    • Effect of anoxia on the induction of α-amylase in cereal seeds
    • P. Perata N. Geshi J. Yamaguchi T. Akazawa Effect of anoxia on the induction of α-amylase in cereal seeds Planta 191 1993 402 408
    • (1993) Planta , vol.191 , pp. 402-408
    • Perata, P.1    Geshi, N.2    Yamaguchi, J.3    Akazawa, T.4
  • 20
    • 0000054574 scopus 로고
    • A proteinase from germinating barley. I. Purification and some physiological properties of a 30 kD cysteine endoproteinase from green malt
    • M. Poulle B.L. Jones A proteinase from germinating barley. I. Purification and some physiological properties of a 30 kD cysteine endoproteinase from green malt Plant Physiol. 88 1988 1454 1460
    • (1988) Plant Physiol. , vol.88 , pp. 1454-1460
    • Poulle, M.1    Jones, B.L.2
  • 22
    • 84897584785 scopus 로고
    • Release and activity of bound β-amylase in a germinating barley grain
    • T. Sopanen C. Lauriere Release and activity of bound β-amylase in a germinating barley grain Plant Physiol. 89 1989 244 249
    • (1989) Plant Physiol. , vol.89 , pp. 244-249
    • Sopanen, T.1    Lauriere, C.2
  • 23
    • 0026034124 scopus 로고
    • A quantitative assessment of the importance of barley seed α-amylase, debranching enzyme, and α-glucosidase in starch degradation
    • Z. Sun C.A. Henson A quantitative assessment of the importance of barley seed α-amylase, debranching enzyme, and α-glucosidase in starch degradation Arch. Biochem. Bioph. 284 1991 298 305
    • (1991) Arch. Biochem. Bioph. , vol.284 , pp. 298-305
    • Sun, Z.1    Henson, C.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.