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Volumn 50, Issue 330, 1999, Pages 63-69

Aldehyde oxidase in roots, leaves and seeds of barley (Hordeum vulgare L.)

Author keywords

Aldehyde oxidase; Barley; Leaves; Molybdenum cofactor (MoCo); Roots; Seeds

Indexed keywords

ANIMALIA; HORDEUM; HORDEUM VULGARE; HORDEUM VULGARE SUBSP. VULGARE; ZEA MAYS;

EID: 0032950253     PISSN: 00220957     EISSN: None     Source Type: Journal    
DOI: 10.1093/jxb/50.330.63     Document Type: Article
Times cited : (37)

References (40)
  • 1
    • 0030096855 scopus 로고    scopus 로고
    • Identification of Ser-453 as the major regulatory phosphorylation site in spinach leaf nitrate reductase
    • Bachmann M, Shiraishi N, Campbell WH, Yoo BC, Harmon AC, Huber SC. 1996. Identification of Ser-453 as the major regulatory phosphorylation site in spinach leaf nitrate reductase. The Plant Cell 8, 505-517.
    • (1996) The Plant Cell , vol.8 , pp. 505-517
    • Bachmann, M.1    Shiraishi, N.2    Campbell, W.H.3    Yoo, B.C.4    Harmon, A.C.5    Huber, S.C.6
  • 2
    • 0000085336 scopus 로고
    • Abscisic acid and cytokinins as possible root-to-shoot signals in xylem sap of rice plants in drying soil
    • Bano A, Dörffling K, Bettin D, Hahn H. 1993. Abscisic acid and cytokinins as possible root-to-shoot signals in xylem sap of rice plants in drying soil. Australian Journal of Plant Physiology 20, 109-115.
    • (1993) Australian Journal of Plant Physiology , vol.20 , pp. 109-115
    • Bano, A.1    Dörffling, K.2    Bettin, D.3    Hahn, H.4
  • 3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0000549163 scopus 로고
    • Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene
    • Deng M, Moureaux T, Caboche M. 1989. Tungstate, a molybdate analog inactivating nitrate reductase, deregulates the expression of the nitrate reductase structural gene. Plant Physiology 91, 304-309.
    • (1989) Plant Physiology , vol.91 , pp. 304-309
    • Deng, M.1    Moureaux, T.2    Caboche, M.3
  • 7
    • 0028134247 scopus 로고
    • Differential response of nitrate reductase and sucrose-phosphate synthase-activation to inorganic and organic salts, in vitro and in situ
    • Huber SC, Huber JL, Kaiser WM. 1994. Differential response of nitrate reductase and sucrose-phosphate synthase-activation to inorganic and organic salts, in vitro and in situ. Physiologia Plantarum 92, 302-310.
    • (1994) Physiologia Plantarum , vol.92 , pp. 302-310
    • Huber, S.C.1    Huber, J.L.2    Kaiser, W.M.3
  • 8
    • 0030879978 scopus 로고    scopus 로고
    • Correlation between apparent activation state of nitrate reductase (NR), NR hysteresis and degradation of NR protein
    • Kaiser WM, Huber SC. 1996. Correlation between apparent activation state of nitrate reductase (NR), NR hysteresis and degradation of NR protein. Journal of Experimental Botany 48, 1367-1374.
    • (1996) Journal of Experimental Botany , vol.48 , pp. 1367-1374
    • Kaiser, W.M.1    Huber, S.C.2
  • 10
    • 0000236687 scopus 로고
    • An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts
    • Koshiba T, Matsuyama H. 1993. An in vitro system of indole-3-acetic acid formation from tryptophan in maize (Zea mays) coleoptile extracts. Plant Physiology 102, 1319-1324.
    • (1993) Plant Physiology , vol.102 , pp. 1319-1324
    • Koshiba, T.1    Matsuyama, H.2
  • 11
    • 0030028266 scopus 로고    scopus 로고
    • Purification and properties of flavin-and molybdenum-containing aldehyde oxidase from coleoptiles of maize
    • Koshiba T, Saito E, Ono N, Yamamoto N, Sato M. 1996. Purification and properties of flavin-and molybdenum-containing aldehyde oxidase from coleoptiles of maize. Plant Physiology 110, 781-789.
    • (1996) Plant Physiology , vol.110 , pp. 781-789
    • Koshiba, T.1    Saito, E.2    Ono, N.3    Yamamoto, N.4    Sato, M.5
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0031424501 scopus 로고    scopus 로고
    • Endogenous biosynthetic precursors of (+)-abscisic acid. V. Inhibition by tungstate and its removal by cinchonine shows that xanthoxal is oxidized by a molybdo-aldehyde oxidase
    • Lee HS, Milborrow BV. 1997. Endogenous biosynthetic precursors of (+)-abscisic acid. V. Inhibition by tungstate and its removal by cinchonine shows that xanthoxal is oxidized by a molybdo-aldehyde oxidase. Australian Journal of Plant Physiology 24, 727-732.
    • (1997) Australian Journal of Plant Physiology , vol.24 , pp. 727-732
    • Lee, H.S.1    Milborrow, B.V.2
  • 14
    • 0029141442 scopus 로고
    • Molybdenum cofactor mutants, specifically impaired in xanthinc dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase
    • Leydecker MT, Moureaux T, Kraepiel Y, Schnorr K, Caboche M. 1995. Molybdenum cofactor mutants, specifically impaired in xanthinc dehydrogenase activity and abscisic acid biosynthesis, simultaneously overexpress nitrate reductase. Plant Physiology 107, 1427-1431.
    • (1995) Plant Physiology , vol.107 , pp. 1427-1431
    • Leydecker, M.T.1    Moureaux, T.2    Kraepiel, Y.3    Schnorr, K.4    Caboche, M.5
  • 15
    • 0030926247 scopus 로고    scopus 로고
    • Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities
    • Marin E, Marion-Poll A. 1997. Tomato flacca mutant is impaired in ABA aldehyde oxidase and xanthine dehydrogenase activities. Plant Physiology and Biochemistry 35, 369-372.
    • (1997) Plant Physiology and Biochemistry , vol.35 , pp. 369-372
    • Marin, E.1    Marion-Poll, A.2
  • 16
    • 0031450614 scopus 로고    scopus 로고
    • Molybdenum cofactor of higher plants: Biosynthesis and molecular biology
    • Mendel RR. 1997. Molybdenum cofactor of higher plants: biosynthesis and molecular biology. Planta 203, 399-405.
    • (1997) Planta , vol.203 , pp. 399-405
    • Mendel, R.R.1
  • 17
    • 0042124819 scopus 로고
    • Assay of molybdenum cofactor of barley
    • Mendel RR, Kirk DW, Wray JL. 1985. Assay of molybdenum cofactor of barley. Phytochemistry 24, 1631-1634.
    • (1985) Phytochemistry , vol.24 , pp. 1631-1634
    • Mendel, R.R.1    Kirk, D.W.2    Wray, J.L.3
  • 19
    • 0028119462 scopus 로고
    • Molybdenum deficiency in wheat results in lower dormancy levels via reduced ABA
    • Modi AT, Cairns ALP. 1994. Molybdenum deficiency in wheat results in lower dormancy levels via reduced ABA. Seed Science Research 4, 329-333.
    • (1994) Seed Science Research , vol.4 , pp. 329-333
    • Modi, A.T.1    Cairns, A.L.P.2
  • 20
    • 0030250857 scopus 로고    scopus 로고
    • Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusiococcin
    • Moorhead G, Douglas P, Morrice N, Scarabel M, Aitken A, Mackintosh C. 1996. Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusiococcin. Current Biology 6, 1104-1113.
    • (1996) Current Biology , vol.6 , pp. 1104-1113
    • Moorhead, G.1    Douglas, P.2    Morrice, N.3    Scarabel, M.4    Aitken, A.5    Mackintosh, C.6
  • 23
    • 0031959530 scopus 로고    scopus 로고
    • Regulation of aldehyde oxidase and nitrate reductase in roots of barley (Hordeum vulgare L.) by nitrogen source and salinity
    • Omarov RT, Sagi M, Lips SH. 1998. Regulation of aldehyde oxidase and nitrate reductase in roots of barley (Hordeum vulgare L.) by nitrogen source and salinity. Journal of Experimental Botany 49, 897-902.
    • (1998) Journal of Experimental Botany , vol.49 , pp. 897-902
    • Omarov, R.T.1    Sagi, M.2    Lips, S.H.3
  • 24
  • 25
    • 84989742281 scopus 로고
    • Metabolism of indole-3-acetaldehyde. III. Some characteristics of aldehyde oxidase of Avena coleoptiles
    • Rajagopal R. 1971. Metabolism of indole-3-acetaldehyde. III. Some characteristics of aldehyde oxidase of Avena coleoptiles. Physiology Plantarum 24, 272-281.
    • (1971) Physiology Plantarum , vol.24 , pp. 272-281
    • Rajagopal, R.1
  • 26
    • 0000490808 scopus 로고
    • Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanum tuberosum)
    • Rothe GM. 1974. Aldehyde oxidase isoenzymes (EC 1.2.3.1) in potato tubers (Solanum tuberosum). Plant Cell Physiology 15, 493-499.
    • (1974) Plant Cell Physiology , vol.15 , pp. 493-499
    • Rothe, G.M.1
  • 27
    • 0032504221 scopus 로고    scopus 로고
    • Xanthine dehydrogenase, nitrate reductase and aldehyde oxidase in ryegrass as affected by nitrogen and salinity
    • in press
    • Sagi M, Omarov RT, Lips SH. 1998. Xanthine dehydrogenase, nitrate reductase and aldehyde oxidase in ryegrass as affected by nitrogen and salinity. Plant Science (in press).
    • (1998) Plant Science
    • Sagi, M.1    Omarov, R.T.2    Lips, S.H.3
  • 28
    • 0030959869 scopus 로고    scopus 로고
    • Nitrate reductase and molybdenum cofactor in annual ryegrass as affected by salinity and nitrogen source
    • Sagi M, Savidov NA, L'vov NP, Lips SH. 1997 Nitrate reductase and molybdenum cofactor in annual ryegrass as affected by salinity and nitrogen source. Physiologia Plantarum 99, 546-553.
    • (1997) Physiologia Plantarum , vol.99 , pp. 546-553
    • Sagi, M.1    Savidov, N.A.2    L'vov, N.P.3    Lips, S.H.4
  • 29
    • 0041577270 scopus 로고    scopus 로고
    • Molybdenum cofactor biosynthesis in two barley (Hordeum vulgare L.) genotypes as affected by nitrate in the tissue and in the growth medium
    • Savidov NA, L'vov NP, Sagi M, Lips SH. 1997a. Molybdenum cofactor biosynthesis in two barley (Hordeum vulgare L.) genotypes as affected by nitrate in the tissue and in the growth medium. Plant Science 122, 51-59.
    • (1997) Plant Science , vol.122 , pp. 51-59
    • Savidov, N.A.1    L'vov, N.P.2    Sagi, M.3    Lips, S.H.4
  • 30
    • 0030909285 scopus 로고    scopus 로고
    • The assay of the molybdenum cofactor in higher plants as affected by pyridine nucleotides and nitrate
    • Savidov NA, Sagi M, Lips SH. 1997b. The assay of the molybdenum cofactor in higher plants as affected by pyridine nucleotides and nitrate. Plant Physiology and Biochemistry 35, 419-426.
    • (1997) Plant Physiology and Biochemistry , vol.35 , pp. 419-426
    • Savidov, N.A.1    Sagi, M.2    Lips, S.H.3
  • 33
    • 0031992097 scopus 로고    scopus 로고
    • Higher activity of an aldehyde oxidase in the auxin-overproducing superrootl mutant of Arabidopsis thaliana
    • Seo M, Akaba Sh, Oritani T, Delarue M, Bellini C, Caboche M, Koshiba T. 1998. Higher activity of an aldehyde oxidase in the auxin-overproducing superrootl mutant of Arabidopsis thaliana. Plant Physiology 116, 687-693.
    • (1998) Plant Physiology , vol.116 , pp. 687-693
    • Seo, M.1    Akaba, Sh.2    Oritani, T.3    Delarue, M.4    Bellini, C.5    Caboche, M.6    Koshiba, T.7
  • 34
    • 0000774435 scopus 로고
    • Abscisic aldehyde is an intermediate in the enzymatic conversion of xanthoxin to abscisic acid in Phaseolus vulgaris L. Leaves
    • Sindhu RK, Griffin DH, Walton DC. 1990. Abscisic aldehyde is an intermediate in the enzymatic conversion of xanthoxin to abscisic acid in Phaseolus vulgaris L. leaves. Plant Physiology 93, 689-694.
    • (1990) Plant Physiology , vol.93 , pp. 689-694
    • Sindhu, R.K.1    Griffin, D.H.2    Walton, D.C.3
  • 35
    • 0345624228 scopus 로고
    • Carbon use efficiency and cell expansion of NaCl-adapted tobacco cells
    • Schnapp S, Bresson R, Hasegawa P. 1990. Carbon use efficiency and cell expansion of NaCl-adapted tobacco cells. Plant Physiology 93, 384-388.
    • (1990) Plant Physiology , vol.93 , pp. 384-388
    • Schnapp, S.1    Bresson, R.2    Hasegawa, P.3
  • 38
    • 0000981896 scopus 로고
    • Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley
    • Walker-Simmons M, Kudra DA, Warner RL. 1989. Reduced accumulation of ABA during water stress in a molybdenum cofactor mutant of barley. Plant Physiology 90, 728-733.
    • (1989) Plant Physiology , vol.90 , pp. 728-733
    • Walker-Simmons, M.1    Kudra, D.A.2    Warner, R.L.3
  • 39
    • 84989695150 scopus 로고
    • Catabolism of indole-3-acetic acid in citrus leaves: Identification and characterization of indole-3-aldehyde oxidase
    • Winer L, Riov J, Goren R. 1993. Catabolism of indole-3-acetic acid in citrus leaves: identification and characterization of indole-3-aldehyde oxidase. Physiologia Plantarum 89, 220-226.
    • (1993) Physiologia Plantarum , vol.89 , pp. 220-226
    • Winer, L.1    Riov, J.2    Goren, R.3
  • 40
    • 77954489275 scopus 로고
    • Long distance transport of abscisic acid in NaCl-treated intact plants of Lupinus albus
    • Wolf O, Jeschke WD, Hartung W. 1990. Long distance transport of abscisic acid in NaCl-treated intact plants of Lupinus albus. Journal of Experimental Botany 41, 593-600.
    • (1990) Journal of Experimental Botany , vol.41 , pp. 593-600
    • Wolf, O.1    Jeschke, W.D.2    Hartung, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.