메뉴 건너뛰기




Volumn 110, Issue 2, 1996, Pages 697-703

Violaxanthin de-epoxidase: Purification of a 43-kilodalton lumenal protein from lettuce by lipid-affinity precipitation with monogalactosyldiacylglyceride

Author keywords

[No Author keywords available]

Indexed keywords

LACTUCA SATIVA;

EID: 0030060496     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.110.2.697     Document Type: Article
Times cited : (103)

References (35)
  • 1
    • 0003956534 scopus 로고
    • Lipid composition of photosynthetic systems
    • TW Goodwin, ed, Academic Press, London
    • Allen CF, Hirayama O, Good P (1966) Lipid composition of photosynthetic systems. In TW Goodwin, ed, Biochemistry of Chloroplasts, Vol I. Academic Press, London, pp 195-200
    • (1966) Biochemistry of Chloroplasts , vol.1 , pp. 195-200
    • Allen, C.F.1    Hirayama, O.2    Good, P.3
  • 2
    • 0017277818 scopus 로고
    • Assay of proteins in the presence of interfering materials
    • Bensadoun A, Weinstein D (1976) Assay of proteins in the presence of interfering materials. Anal Biochem 70: 241-250
    • (1976) Anal Biochem , vol.70 , pp. 241-250
    • Bensadoun, A.1    Weinstein, D.2
  • 3
    • 0001848758 scopus 로고
    • Regulation of photosynthetic light energy capture, conversion, and dissipation in leaves of higher plants
    • ED Schulze, M Caldwell, eds, Springer-Verlag, New York
    • Björkman O, Demmig-Adams B (1993) Regulation of photosynthetic light energy capture, conversion, and dissipation in leaves of higher plants, In ED Schulze, M Caldwell, eds, Ecological Studies, Vol 100. Springer-Verlag, New York, pp 14-47
    • (1993) Ecological Studies , vol.100 , pp. 14-47
    • Björkman, O.1    Demmig-Adams, B.2
  • 5
    • 9444221725 scopus 로고
    • Reversed micelles for protein purification
    • TT Ngo, ed, Plenum Press, New York
    • Dekker M (1993) Reversed micelles for protein purification. In TT Ngo, ed, Molecular Interactions in Bioseparations. Plenum Press, New York, pp 533-544
    • (1993) Molecular Interactions in Bioseparations , pp. 533-544
    • Dekker, M.1
  • 7
    • 0002368978 scopus 로고
    • Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching
    • Gilmore AM, Yamamoto HY (1993) Linear models relating xanthophylls and lumen acidity to non-photochemical fluorescence quenching. Evidence that antheraxanthin explains zeaxanthin-independent quenching. Photosynth Res 35: 67-78
    • (1993) Photosynth Res , vol.35 , pp. 67-78
    • Gilmore, A.M.1    Yamamoto, H.Y.2
  • 8
    • 48749149469 scopus 로고
    • Monogalactosyldiacylglycerol: The most abundant polar lipid in nature
    • Gounaris, K, Barber J (1983) Monogalactosyldiacylglycerol: the most abundant polar lipid in nature. Trends Biochem Sci 8: 378-381
    • (1983) Trends Biochem Sci , vol.8 , pp. 378-381
    • Gounaris, K.1    Barber, J.2
  • 9
    • 0001227304 scopus 로고
    • Lichtbedingte pH-Erniedringung in einem Chloroplasten-Kompartiment als Ursache der enzymatischen Violaxanthin- → Zeaxanthin-Umwandlung; Beziehungen zur Photophosphorylierung
    • Hager A (1969) Lichtbedingte pH-Erniedringung in einem Chloroplasten-Kompartiment als Ursache der enzymatischen Violaxanthin- → Zeaxanthin-Umwandlung; Beziehungen zur Photophosphorylierung. Planta 89: 224-243
    • (1969) Planta , vol.89 , pp. 224-243
    • Hager, A.1
  • 10
    • 85006828126 scopus 로고
    • Die reversiblen, lightabhängigen Xanthophyllum-wandlungen im Chloroplasten
    • Hager A (1975) Die reversiblen, lightabhängigen Xanthophyllum-wandlungen im Chloroplasten. Ber Dtsch Bot Ges 88: 27-44
    • (1975) Ber Dtsch Bot Ges , vol.88 , pp. 27-44
    • Hager, A.1
  • 11
    • 0028004703 scopus 로고
    • Localizaion of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease
    • Hager A, Holocher K (1994) Localizaion of the xanthophyll-cycle enzyme violaxanthin de-epoxidase within the thylakoid lumen and abolition of its mobility by a (light-dependent) pH decrease. Planta 192: 581-589
    • (1994) Planta , vol.192 , pp. 581-589
    • Hager, A.1    Holocher, K.2
  • 12
    • 0000899175 scopus 로고
    • Veränderung der Lichtabsorption eines Carotinoids im Enzym(De-epoxidase)-Substrat(Violaxanthin)-Komplex
    • Hager A, Perz H (1970) Veränderung der Lichtabsorption eines Carotinoids im Enzym(De-epoxidase)-Substrat(Violaxanthin)-Komplex. Planta 93: 314-322
    • (1970) Planta , vol.93 , pp. 314-322
    • Hager, A.1    Perz, H.2
  • 13
    • 0000647672 scopus 로고
    • Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant
    • Hilhorst R, Laane C, Veeger C (1983) Enzymatic conversion of apolar compounds in organic media using an NADH-regenerating system and dihydrogen as reductant. FEBS Lett 159: 225-228
    • (1983) FEBS Lett , vol.159 , pp. 225-228
    • Hilhorst, R.1    Laane, C.2    Veeger, C.3
  • 14
    • 0028006047 scopus 로고
    • Regulation of light harvesting in green plants. Indication by nonphotochemical quenching of chlorophyll fluorescence
    • Horton P, Ruban AV, Walters RG (1994) Regulation of light harvesting in green plants. Indication by nonphotochemical quenching of chlorophyll fluorescence. Plant Physiol 106: 415-420
    • (1994) Plant Physiol , vol.106 , pp. 415-420
    • Horton, P.1    Ruban, A.V.2    Walters, R.G.3
  • 15
    • 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
  • 17
    • 0001757622 scopus 로고
    • Characterization of the heat shock response in cultured sugarcane cells. 1. Physiology of the heat shock response and heat shock protein synthesis
    • Moisyadi S, Harrington HM (1989) Characterization of the heat shock response in cultured sugarcane cells. 1. Physiology of the heat shock response and heat shock protein synthesis. Plant Physiol 90: 1156-1162
    • (1989) Plant Physiol , vol.90 , pp. 1156-1162
    • Moisyadi, S.1    Harrington, H.M.2
  • 18
    • 0000629113 scopus 로고
    • Mehler-peroxidase reaction mediates zeaxanthin formation and zeaxanthin-related fluorescence quenching in intact chloroplasts
    • Neubauer C, Yamamoto HY (1992) Mehler-peroxidase reaction mediates zeaxanthin formation and zeaxanthin-related fluorescence quenching in intact chloroplasts. Plant Physiol 99: 1354-1361
    • (1992) Plant Physiol , vol.99 , pp. 1354-1361
    • Neubauer, C.1    Yamamoto, H.Y.2
  • 19
    • 0028150268 scopus 로고
    • Membrane barriers and Mehler-peroxidase reaction limit the ascorbate available for violaxanthin de-epoxidase activity in intact chloroplasts
    • Neubauer C, Yamamoto HY (1994) Membrane barriers and Mehler-peroxidase reaction limit the ascorbate available for violaxanthin de-epoxidase activity in intact chloroplasts. Photosynth Res 39: 137-147
    • (1994) Photosynth Res , vol.39 , pp. 137-147
    • Neubauer, C.1    Yamamoto, H.Y.2
  • 20
    • 0026056608 scopus 로고
    • Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins
    • Peter GF, Thornber JP (1991) Biochemical composition and organization of higher plant photosystem II light-harvesting pigment-proteins. J Biol Chem 266: 16745-16754
    • (1991) J Biol Chem , vol.266 , pp. 16745-16754
    • Peter, G.F.1    Thornber, J.P.2
  • 21
    • 0028310069 scopus 로고
    • Regulation and possible function of the violaxanthin cycle
    • Pfündel E, Bilger W (1994) Regulation and possible function of the violaxanthin cycle. Photosynth Res 42: 89-109
    • (1994) Photosynth Res , vol.42 , pp. 89-109
    • Pfündel, E.1    Bilger, W.2
  • 22
    • 0006253162 scopus 로고
    • Purification of violaxanthin de-epoxidase by lipid affinity precipitation
    • HY Yamamoto, CM Smith, eds, American Society of Plant Physiologists, Rockville, MD
    • Rockholm DC, Yamamoto HY (1993) Purification of violaxanthin de-epoxidase by lipid affinity precipitation. In HY Yamamoto, CM Smith, eds, Photosynthetic Responses to the Environment. American Society of Plant Physiologists, Rockville, MD, p 237
    • (1993) Photosynthetic Responses to the Environment , pp. 237
    • Rockholm, D.C.1    Yamamoto, H.Y.2
  • 23
    • 0001001691 scopus 로고
    • Change in the interrelationship of the basic carotenoids of the plastids of green leaves under the action of light
    • Sapozhnikov DI, Krasovskaya TA, Maevskaya AN (1957) Change in the interrelationship of the basic carotenoids of the plastids of green leaves under the action of light. Dokl Akad Nauk USSR 113: 465-467
    • (1957) Dokl Akad Nauk USSR , vol.113 , pp. 465-467
    • Sapozhnikov, D.I.1    Krasovskaya, T.A.2    Maevskaya, A.N.3
  • 24
    • 0016162088 scopus 로고
    • Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. III. Reaction kinetics and effect of light intensity on de-epoxidase activity and substrate availability
    • Siefermann D, Yamamoto HY (1974) Light-induced de-epoxidation of violaxanthin in lettuce chloroplasts. III. Reaction kinetics and effect of light intensity on de-epoxidase activity and substrate availability. Biochim Biophys Acta 357: 144-150
    • (1974) Biochim Biophys Acta , vol.357 , pp. 144-150
    • Siefermann, D.1    Yamamoto, H.Y.2
  • 25
    • 0000484207 scopus 로고
    • Reassembly of solubilized chlorophyll-protein complexes in proteolipid particles - Comparison of monogalactosyldiacylglycerol and two phospholipids
    • Siefermann-Harms D, Ninnemann H, Yamamoto HY (1987) Reassembly of solubilized chlorophyll-protein complexes in proteolipid particles - comparison of monogalactosyldiacylglycerol and two phospholipids. Biochim Biophys Acta 892: 303-313
    • (1987) Biochim Biophys Acta , vol.892 , pp. 303-313
    • Siefermann-Harms, D.1    Ninnemann, H.2    Yamamoto, H.Y.3
  • 26
    • 0000502622 scopus 로고
    • Reconstitution by monogalactosyldiacylglycerol of energy transfer from light-harvesting chlorophyll a/b-protein complex to the photosystems in Triton X-100-solubilized thylakoids
    • Siefermann-Harms D, Ross JW, Kaneshiro KH, Yamamoto HY (1982) Reconstitution by monogalactosyldiacylglycerol of energy transfer from light-harvesting chlorophyll a/b-protein complex to the photosystems in Triton X-100-solubilized thylakoids. FEBS Lett 149: 191-196
    • (1982) FEBS Lett , vol.149 , pp. 191-196
    • Siefermann-Harms, D.1    Ross, J.W.2    Kaneshiro, K.H.3    Yamamoto, H.Y.4
  • 27
    • 0000959808 scopus 로고
    • Leaf xanthophyll content and composition in sun and shade leaves determined by HPLC
    • Thayer SS, Björkman O (1990) Leaf xanthophyll content and composition in sun and shade leaves determined by HPLC. Photosynth Res 23: 331-343
    • (1990) Photosynth Res , vol.23 , pp. 331-343
    • Thayer, S.S.1    Björkman, O.2
  • 29
    • 0000171640 scopus 로고
    • Xanthophyll cycles
    • Yamamoto HY (1985) Xanthophyll cycles. Methods Enzymol 110: 303-312
    • (1985) Methods Enzymol , vol.110 , pp. 303-312
    • Yamamoto, H.Y.1
  • 30
    • 0000882260 scopus 로고
    • Carotenoids: Localization and function
    • DR Ort, DF Yocum, eds, Kluwer Academic, Dordrecht, The Netherlands (in press)
    • Yamamoto HY, Bassi R (1995) Carotenoids: localization and function. In DR Ort, DF Yocum, eds, Oxygenic Photosynthesis: The Light Reactions. Kluwer Academic, Dordrecht, The Netherlands (in press)
    • (1995) Oxygenic Photosynthesis: The Light Reactions
    • Yamamoto, H.Y.1    Bassi, R.2
  • 32
    • 0018129919 scopus 로고
    • Violaxanthin de-epoxidase: Lipid composition and substrate specificity
    • Yamamoto HY, Higashi RM (1978) Violaxanthin de-epoxidase: lipid composition and substrate specificity. Arch Biochem Biophys 190: 514-522
    • (1978) Arch Biochem Biophys , vol.190 , pp. 514-522
    • Yamamoto, H.Y.1    Higashi, R.M.2
  • 33
    • 0015520731 scopus 로고
    • The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region
    • Yamamoto HY, Kamite L (1972) The effects of dithiothreitol on violaxanthin de-epoxidation and absorbance changes in the 500 nm region. Biochim Biophys Acta 267: 538-543
    • (1972) Biochim Biophys Acta , vol.267 , pp. 538-543
    • Yamamoto, H.Y.1    Kamite, L.2
  • 34
    • 0001504653 scopus 로고
    • An ascorbate-induced absorbance change in chloroplasts from violaxanthin de-epoxidation
    • Yamamoto HY, Kamite L, Wang YY (1972) An ascorbate-induced absorbance change in chloroplasts from violaxanthin de-epoxidation. Plant Physiol 49: 224-228
    • (1972) Plant Physiol , vol.49 , pp. 224-228
    • Yamamoto, H.Y.1    Kamite, L.2    Wang, Y.Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.