메뉴 건너뛰기
Plant Physiology
Volumn 113, Issue 1, 1997, Pages 243-248
Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco
Author keywords

[No Author keywords available]
Indexed keywords

BOVINAE;
EID: 0031040836     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.113.1.243     Document Type: Article
Times cited : (77)
References (22)
  • 1
    • 0006875655 scopus 로고
    • A role for ribulose-1,5-bisphosphate carboxylase as a metabolite buffer
    • Ashton AR (1982) A role for ribulose-1,5-bisphosphate carboxylase as a metabolite buffer. FEBS Lett 145: 1-7
    • (1982) FEBS Lett , vol.145 , pp. 1-7
    • Ashton, A.R.1
  • 2
    • 0025281866 scopus 로고
    • Study of strong to ultratight protein interactions using differential scanning calorimetry
    • Brandts JF, Lin L-N (1990) Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry 29: 6927-6940
    • (1990) Biochemistry , vol.29 , pp. 6927-6940
    • Brandts, J.F.1    Lin, L.-N.2
  • 3
    • 0001276970 scopus 로고
    • Protein-bound ribulose bisphosphate correlates with deactivation of ribulose bisphosphate carboxylase in leaves
    • Brooks A, Portis AR Jr (1988) Protein-bound ribulose bisphosphate correlates with deactivation of ribulose bisphosphate carboxylase in leaves. Plant Physiol 87: 244-249
    • (1988) Plant Physiol , vol.87 , pp. 244-249
    • Brooks, A.1    Portis Jr., A.R.2
  • 4
    • 11944267330 scopus 로고
    • A kinetic characterization of slow inactivation of ribulosebisphosphate carboxylase during catalysis
    • Edmondson DL, Badger MR, Andrews TJ (1990a) A kinetic characterization of slow inactivation of ribulosebisphosphate carboxylase during catalysis. Plant Physiol 93: 1376-1382
    • (1990) Plant Physiol , vol.93 , pp. 1376-1382
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 5
    • 0001041057 scopus 로고
    • Slow inactivation of ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site
    • Edmondson DL, Badger MR, Andrews TJ (1990b) Slow inactivation of ribulosebisphosphate carboxylase during catalysis is caused by accumulation of a slow, tight-binding inhibitor at the catalytic site. Plant Physiol 93: 1390-1397
    • (1990) Plant Physiol , vol.93 , pp. 1390-1397
    • Edmondson, D.L.1    Badger, M.R.2    Andrews, T.J.3
  • 6
    • 0342561548 scopus 로고    scopus 로고
    • Differential effects of N- and C-terminal deletions on the two activities of Rubisco activase
    • Esau BD, Snyder GW, Portis AR Jr (1996) Differential effects of N- and C-terminal deletions on the two activities of Rubisco activase. Arch Biochem Biophys 326: 100-105
    • (1996) Arch Biochem Biophys , vol.326 , pp. 100-105
    • Esau, B.D.1    Snyder, G.W.2    Portis Jr., A.R.3
  • 7
    • 85036448012 scopus 로고    scopus 로고
    • Heat treatment inhibits light activation of Rubisco by Rubisco activase
    • abstract no. 346
    • Feller U, Crafts-Brandner S, Salvucci ME (1996) Heat treatment inhibits light activation of Rubisco by Rubisco activase (abstract no. 346). Plant Physiol 111: S-94
    • (1996) Plant Physiol , vol.111
    • Feller, U.1    Crafts-Brandner, S.2    Salvucci, M.E.3
  • 8
    • 0022552149 scopus 로고
    • Expression of wild-type and mutant forms of influenza hemagglutinin: The role of folding in intracellular transport
    • Gething M-J, McCammon K, Sambrook J (1986) Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport. Cell 46: 939-950
    • (1986) Cell , vol.46 , pp. 939-950
    • Gething, M.-J.1    McCammon, K.2    Sambrook, J.3
  • 9
    • 0002393676 scopus 로고
    • Influences of leaf temperature on photosynthetic carbon metabolism in wheat
    • Kobza J, Edwards GE (1987) Influences of leaf temperature on photosynthetic carbon metabolism in wheat. Plant Physiol 83: 69-74
    • (1987) Plant Physiol , vol.83 , pp. 69-74
    • Kobza, J.1    Edwards, G.E.2
  • 10
    • 0000432216 scopus 로고
    • Regulation of ribulose-1,5-bisphosphate carboxylase activity in response to diurnal changes in irradiance
    • Kobza J, Seeman JR (1989) Regulation of ribulose-1,5-bisphosphate carboxylase activity in response to diurnal changes in irradiance. Plant Physiol 89: 918-924
    • (1989) Plant Physiol , vol.89 , pp. 918-924
    • Kobza, J.1    Seeman, J.R.2
  • 11
    • 0016168192 scopus 로고
    • An improved spectrophotometric assay for ribulosebisphosphate carboxylase
    • Lilley RM, Walker DA (1974) An improved spectrophotometric assay for ribulosebisphosphate carboxylase. Biochim Biophys Acta 358: 226-229
    • (1974) Biochim Biophys Acta , vol.358 , pp. 226-229
    • Lilley, R.M.1    Walker, D.A.2
  • 12
    • 0020348141 scopus 로고
    • Ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach, tomato or tobacco leaves
    • McCurry SD, Gee R, Tolbert NE (1982) Ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach, tomato or tobacco leaves. Methods Enzymol 90: 515-521
    • (1982) Methods Enzymol , vol.90 , pp. 515-521
    • McCurry, S.D.1    Gee, R.2    Tolbert, N.E.3
  • 13
    • 0000384908 scopus 로고
    • Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase activity
    • Portis AR Jr (1992) Regulation of ribulose-1,5-bisphosphate carboxylase/oxygenase activity. Annu Rev Plant Physiol Plant Mol Biol 43: 415-437
    • (1992) Annu Rev Plant Physiol Plant Mol Biol , vol.43 , pp. 415-437
    • Portis Jr., A.R.1
  • 14
    • 0024485948 scopus 로고
    • Adenosine triphosphate hydrolysis by purified Rubisco activase
    • Robinson SP, Portis AR Jr (1989) Adenosine triphosphate hydrolysis by purified Rubisco activase. Arch Biochem Biophys 268: 93-99
    • (1989) Arch Biochem Biophys , vol.268 , pp. 93-99
    • Robinson, S.P.1    Portis Jr., A.R.2
  • 15
    • 34250112628 scopus 로고
    • A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo
    • Salvucci ME, Portis AR Jr, Ogren WL (1985) A soluble chloroplast protein catalyzes ribulosebisphosphate carboxylase/oxygenase activation in vivo. Photosynth Res 7: 193-201
    • (1985) Photosynth Res , vol.7 , pp. 193-201
    • Salvucci, M.E.1    Portis Jr., A.R.2    Ogren, W.L.3
  • 17
    • 0028910189 scopus 로고
    • Rubisco activase, a possible new member of the molecular chaperone family
    • Sánchez de Jiménez E, Medrano L, Martinez-Barajas E (1995) Rubisco activase, a possible new member of the molecular chaperone family. Biochemistry 34: 2826-2831
    • (1995) Biochemistry , vol.34 , pp. 2826-2831
    • Sánchez De Jiménez, E.1    Medrano, L.2    Martinez-Barajas, E.3
  • 18
    • 0029203156 scopus 로고
    • Differential scanning calorimetry of proteins
    • Sanchez-Ruiz JM (1995) Differential scanning calorimetry of proteins. Subcell Biochem 24: 133-176
    • (1995) Subcell Biochem , vol.24 , pp. 133-176
    • Sanchez-Ruiz, J.M.1
  • 19
    • 0000266632 scopus 로고
    • 2, and mercurials on the circular dichroism, thermal stability, and light scattering of ribulose 1,5-bisphosphate carboxylase from alfalfa, spinach and tobacco
    • 2, and mercurials on the circular dichroism, thermal stability, and light scattering of ribulose 1,5-bisphosphate carboxylase from alfalfa, spinach and tobacco. Plant Physiol 68: 808-813
    • (1981) Plant Physiol , vol.68 , pp. 808-813
    • Tomimatsu, Y.1    Donovan, J.W.2
  • 20
    • 0001616104 scopus 로고
    • Species-dependent variation in the interaction of substrate-bound ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase
    • Wang Z-Y, Snyder GW, Esau BD, Portis AR Jr, Ogren WL (1992) Species-dependent variation in the interaction of substrate-bound ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and Rubisco activase. Plant Physiol 100: 1858-1862
    • (1992) Plant Physiol , vol.100 , pp. 1858-1862
    • Wang, Z.-Y.1    Snyder, G.W.2    Esau, B.D.3    Portis Jr., A.R.4    Ogren, W.L.5
  • 21
    • 0000687223 scopus 로고
    • The temperature-sensitivity of dark-inactivation and light-inactivation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts
    • Weis E (1981a) The temperature-sensitivity of dark-inactivation and light-inactivation of the ribulose-1,5-bisphosphate carboxylase in spinach chloroplasts. FEBS Lett 129: 197-200
    • (1981) FEBS Lett , vol.129 , pp. 197-200
    • Weis, E.1
  • 22
    • 0002473289 scopus 로고
    • Reversible heat-inactivation of the Calvin cycle: A possible mechanism of the temperature regulation of photosynthesis
    • Weis E (1981b) Reversible heat-inactivation of the Calvin cycle: a possible mechanism of the temperature regulation of photosynthesis. Planta 151: 33-39
    • (1981) Planta , vol.151 , pp. 33-39
    • Weis, E.1

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.