메뉴 건너뛰기




Volumn 225, Issue 3-4, 2005, Pages 235-242

Both chloroplastic and cytosolic phosphofructoaldolase isozymes are present in the pea leaf nucleus

Author keywords

Fructose 1,6 bisphosphate aldolase; Isozyme; Multifunctional enzyme; Nuclear protein; Pisum sativum

Indexed keywords

FRUCTOSE BISPHOSPHATE ALDOLASE; ISOENZYME;

EID: 26844451007     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-005-0099-1     Document Type: Article
Times cited : (14)

References (21)
  • 1
    • 0042836670 scopus 로고    scopus 로고
    • A quantitative method for assessing co-localization in immuno-labeled thin section electron micrographs.
    • JB Anderson AA Carol VK Brown LE Anderson 2003 A quantitative method for assessing co-localization in immuno-labeled thin section electron micrographs. J Struct Biol 143 95 106
    • (2003) J Struct Biol , vol.143 , pp. 95-106
    • Anderson, J.B.1    Carol, A.A.2    Brown, V.K.3    Anderson, L.E.4
  • 2
    • 1242323414 scopus 로고    scopus 로고
    • Seven enzymes of carbon metabolism, including three Calvin cycle isozymes, are present in the secondary cell wall thickenings of the developing xylem tracheary elements in pea leaves.
    • LE Anderson AA Carol 2004 Seven enzymes of carbon metabolism, including three Calvin cycle isozymes, are present in the secondary cell wall thickenings of the developing xylem tracheary elements in pea leaves. Int J Plant Sci 165 243 256
    • (2004) Int J Plant Sci , vol.165 , pp. 243-256
    • Anderson, L.E.1    Carol, A.A.2
  • 3
    • 0016733824 scopus 로고
    • Chloroplast and cytoplasmic enzymes: Subunit structure of pea leaf aldolases
    • - Heinrikson RL, Noyes C (1975) Chloroplast and cytoplasmic enzymes: subunit structure of pea leaf aldolases. Arch Biochem Biophys 169: 262-268
    • (1975) Arch Biochem Biophys , vol.169 , pp. 262-268
    • Heinrikson, R.L.1    Noyes, C.2
  • 4
    • 0029310579 scopus 로고
    • Three enzymes of carbon metabolism, or their antigenic analogs, in pea nuclei
    • - Wang X, Gibbons JT (1995a) Three enzymes of carbon metabolism, or their antigenic analogs, in pea nuclei. Plant Physiol 108: 659-667
    • (1995) Plant Physiol , vol.108 , pp. 659-667
    • Wang, X.1    Gibbons, J.T.2
  • 5
    • 0029108853 scopus 로고
    • Enzyme-enzyme interaction in the chloroplast: Glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase
    • - Goldhaber-Gordon IM, Li D, Tang X-Y, Xiang M, Prakash N (1995b) Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase. Planta 196: 245-255
    • (1995) Planta , vol.196 , pp. 245-255
    • Goldhaber-Gordon, I.M.1    Li, D.2    Tang, X.-Y.3    Xiang, M.4    Prakash, N.5
  • 6
    • 1242298754 scopus 로고    scopus 로고
    • Both chloroplastic and cytosolic fructose bisphosphatase isozymes are present in the pea leaf nucleus
    • - Yousefzai R, Ringenberg MR, Carol AA (2004a) Both chloroplastic and cytosolic fructose bisphosphatase isozymes are present in the pea leaf nucleus. Plant Sci 166: 721-730
    • (2004) Plant Sci , vol.166 , pp. 721-730
    • Yousefzai, R.1    Ringenberg, M.R.2    Carol, A.A.3
  • 7
    • 3142641336 scopus 로고    scopus 로고
    • Both chloroplastic and cytosolic phosphoglycerate kinase isozymes are present in the pea leaf nucleus
    • - Bryant JA, Carol AA (2004b) Both chloroplastic and cytosolic phosphoglycerate kinase isozymes are present in the pea leaf nucleus. Protoplasma 223: 103-110
    • (2004) Protoplasma , vol.223 , pp. 103-110
    • Bryant, J.A.1    Carol, A.A.2
  • 8
    • 1242323413 scopus 로고    scopus 로고
    • Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus
    • - Ringenberg MR, Carol AA (2004c) Cytosolic glyceraldehyde-3-P dehydrogenase and the B subunit of the chloroplast enzyme are present in the pea leaf nucleus. Protoplasma 223: 33-43
    • (2004) Protoplasma , vol.223 , pp. 33-43
    • Ringenberg, M.R.1    Carol, A.A.2
  • 10
    • 0036016851 scopus 로고    scopus 로고
    • Isolation of rice genes possibly involved in the photoperiodic control of flowering by a fluorescent differential display method.
    • R Hayama T Izawa K Shimamoto 2002 Isolation of rice genes possibly involved in the photoperiodic control of flowering by a fluorescent differential display method. Plant Cell Physiol 43 494 504
    • (2002) Plant Cell Physiol , vol.43 , pp. 494-504
    • Hayama, R.1    Izawa, T.2    Shimamoto, K.3
  • 11
    • 0035698788 scopus 로고    scopus 로고
    • Many but not all genes in Chlamydomonas reinhardtii are regulated by the circadian clock.
    • S Jacobshagen JR Whetstine JM Boling 2001 Many but not all genes in Chlamydomonas reinhardtii are regulated by the circadian clock. Plant Biol 3 592 597
    • (2001) Plant Biol , vol.3 , pp. 592-597
    • Jacobshagen, S.1    Whetstine, J.R.2    Boling, J.M.3
  • 12
    • 0036403312 scopus 로고    scopus 로고
    • RNA-protein interactions of the 3′ untranslated regions of myosin heavy chain transcripts.
    • A Kiri G Goldspink 2002 RNA-protein interactions of the 3′ untranslated regions of myosin heavy chain transcripts. J Muscle Res Cell Motil 23 119 129
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 119-129
    • Kiri, A.1    Goldspink, G.2
  • 13
    • 0035022018 scopus 로고    scopus 로고
    • Exquisite specificity and peptide epitope recognition promiscuity, properties shared by antibodies from sharks to humans.
    • JJ Marchalonis MK Adelman IF Robey SF Schluter AB Edmundson 2001 Exquisite specificity and peptide epitope recognition promiscuity, properties shared by antibodies from sharks to humans. J Mol Recognit 14 110 121
    • (2001) J Mol Recognit , vol.14 , pp. 110-121
    • Marchalonis, J.J.1    Adelman, M.K.2    Robey, I.F.3    Schluter, S.F.4    Edmundson, A.B.5
  • 16
    • 0026630489 scopus 로고
    • Chloroplast and cytoplasmic enzymes: Isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases.
    • K Razdan RL Heinrikson H Zurcher-Neely PW Morris LE Anderson 1992 Chloroplast and cytoplasmic enzymes: isolation and sequencing of cDNAs coding for two distinct pea chloroplast aldolases. Arch Biochem Biophys 298 192 197
    • (1992) Arch Biochem Biophys , vol.298 , pp. 192-197
    • Razdan, K.1    Heinrikson, R.L.2    Zurcher-Neely, H.3    Morris, P.W.4    Anderson, L.E.5
  • 19
    • 0342264393 scopus 로고    scopus 로고
    • Subcellular localization of aldolase B.
    • DE Saez JC Slebe 2000 Subcellular localization of aldolase B. J Cell Biochem 78 62 72
    • (2000) J Cell Biochem , vol.78 , pp. 62-72
    • Saez, D.E.1    Slebe, J.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.