메뉴 건너뛰기




Volumn 124, Issue 1, 2000, Pages 321-330

NADPH supply and mannitol biosynthesis. Characterization, cloning, and regulation of the non-reversible glyceraldehyde-3-phosphate dehydrogenase in celery leaves

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID SEQUENCE; CLONE; COMPLEMENTARY DNA; CULTIVAR; CYTOSOL; ENZYME REGULATION; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; IN VITRO CULTURE; MANNITOL; MANNOSE 6 PHOSPHATE REDUCTASE; MESSENGER RNA; MOLECULAR WEIGHT; NON REVERSIBLE GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; OPEN READING FRAME; POLYMERASE CHAIN REACTION; SDS POLYACRYLAMIDE GEL ELECTROPHORESIS;

EID: 0033830281     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.124.1.321     Document Type: Article
Times cited : (49)

References (29)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0000954734 scopus 로고
    • Mannose-6-phosphate reductase, a key enzyme in photoassimilate partitioning, is abundant and located in the cytosol of photosynthetically active cells of celery (Apium graveolens L.) source leaves
    • (1993) Plant Physiol , vol.102 , pp. 345-356
    • Everard, J.D.1    Franceschi, V.R.2    Loescher, W.H.3
  • 7
    • 0028330227 scopus 로고
    • Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH
    • (1994) J Mol Biol , vol.237 , pp. 165-171
    • Habenicht, A.1    Hellman, U.2    Cerff, R.3
  • 8
    • 0023958431 scopus 로고
    • Purification and kinetic and structural properties of spinach leaf NADP-dependent nonphorylating glyceraldehyde-3-phosphate dehydrogenase
    • (1988) Arch Biochem Biophys , vol.260 , pp. 830-840
    • Iglesias, A.A.1    Losada, M.2
  • 10
    • 0014949207 scopus 로고
    • Cleavage of structural protein during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0001800421 scopus 로고    scopus 로고
    • Sugar alcohol metabolism in sinks and sources
    • E Zamski, AA Schaffer, eds, Photoassimilate Distribution in Plant and Crops: Source-Sink Relationships. Marcel Dekker, New York
    • (1996) , pp. 185-207
    • Loescher, W.H.1    Everard, J.D.2
  • 14
    • 0001704090 scopus 로고    scopus 로고
    • Regulation of sugar alcohol biosynthesis
    • RC Leegood, TD Sharkey, S von Caemmerer, eds, Photosynthesis: Physiology and Metabolism. Kluwer Academic Publisher, Dordrecht, The Netherlands
    • (2000) , pp. 275-299
    • Loescher, W.H.1    Everard, J.D.2
  • 18
    • 0001730693 scopus 로고
    • Measurement by enzymatic cycling
    • HU Bergmeyer, ed, Methods of Enzymatic Analysis, Vol 4. Verlag Chemie International, Deerfield Beach, FL
    • (1974) , pp. 2059-2072
    • Passonneau, J.V.1    Lowry, O.H.2
  • 22
    • 0008041972 scopus 로고
    • Biochemical Calculations, 2nd Ed. John Wiley and Sons, New York
    • (1976) , pp. 246-273
    • Segel, I.H.1
  • 25
    • 0004502198 scopus 로고
    • The flux of carbon between chloroplast and cytoplasm
    • DT Dennis, DH Turpin, eds, Plant Physiology, Biochemistry and Molecular Biology. John Wiley and Sons, New York
    • (1990) , pp. 309-326
    • Stitt, M.1
  • 29
    • 0027520216 scopus 로고
    • + oxidoreductase (nonphosphorylating) by adenylate compounds: The effect of dead-end inhibitors on a steady state random reaction mechanism
    • (1993) Arch Biochem Biophys , vol.306 , pp. 76-82
    • Trost, P.1    Pupillo, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.