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Abstract:

Kinetic analysis of glyceraldehyde-3-phosphate dehydrogenase showed that the enhancement of the NADP-linked activity by specific chloroplast modulators is a concerted process; either a selected second metabolite or the couple dithiothreitol/thioredoxin-f lowers the concentration of primary modulators (ATP, NADPH, inorganic phosphate, 1,3-diphosphoglycerate) required for maximal stimulation (A0.5). Organic solvents also stimulate NADP-glyceraldehyde-3-phosphate dehydrogenase in the absence of any modulator; the concentration for the highest specific activity correlates inversely with the respective octanol-water partition coefficient. On the other hand, alcohols also enhance enzyme activity by lowering the A0.5 for primary modulators. Another compound-spermine-inhibits both the ATP- and the inorganic phosphate-mediated activation, but it does not influence the NADPH-induced process. © 1986.

Registro:

Documento: Artículo
Título:Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis
Autor:Wolosiuk, R.A.; Hertig, C.M.; Busconi, L.
Filiación:Instituto de Investigaciones Bioquimicas, Facultad de Ciencias Exactas y Naturales (UBA), Antonio Machado 151, 1405 Buenos Aires, Argentina
Palabras clave:adenosine triphosphate; alcohol derivative; dithiothreitol; glyceraldehyde 3 phosphate dehydrogenase; Glyceraldehyde 3 Phosphate Dehydrogenases; nicotinamide adenine dinucleotide phosphate; phosphate; propanol; solvent; spermine; thioredoxin f; vegetable protein; article; chloroplast; drug effect; enzyme activation; enzymology; metabolism; plant; 1-Propanol; Adenosine Triphosphate; Alcohols; Chloroplasts; Dithiothreitol; Enzyme Activation; Glyceraldehyde-3-Phosphate Dehydrogenases; NADP; Phosphates; Plant Proteins; Plants; Solvents; Spermine
Año:1986
Volumen:246
Número:1
Página de inicio:1
Página de fin:8
DOI: http://dx.doi.org/10.1016/0003-9861(86)90443-1
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:adenosine triphosphate, 15237-44-2, 56-65-5, 987-65-5; dithiothreitol, 3483-12-3; glyceraldehyde 3 phosphate dehydrogenase, 9001-50-7; nicotinamide adenine dinucleotide phosphate, 53-59-8; phosphate, 14066-19-4, 14265-44-2; propanol, 62309-51-7, 71-23-8; spermine, 306-67-2, 71-44-3; 1-Propanol, 71-23-8; Adenosine Triphosphate, 56-65-5; Alcohols; Dithiothreitol, 3483-12-3; Glyceraldehyde-3-Phosphate Dehydrogenases, EC 1.2.1.-; NADP, 53-59-8; Phosphates; Plant Proteins; Solvents; Spermine, 71-44-3; thioredoxin f
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v246_n1_p1_Wolosiuk

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Citas:

---------- APA ----------
Wolosiuk, R.A., Hertig, C.M. & Busconi, L. (1986) . Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis. Archives of Biochemistry and Biophysics, 246(1), 1-8.
http://dx.doi.org/10.1016/0003-9861(86)90443-1
---------- CHICAGO ----------
Wolosiuk, R.A., Hertig, C.M., Busconi, L. "Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis" . Archives of Biochemistry and Biophysics 246, no. 1 (1986) : 1-8.
http://dx.doi.org/10.1016/0003-9861(86)90443-1
---------- MLA ----------
Wolosiuk, R.A., Hertig, C.M., Busconi, L. "Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis" . Archives of Biochemistry and Biophysics, vol. 246, no. 1, 1986, pp. 1-8.
http://dx.doi.org/10.1016/0003-9861(86)90443-1
---------- VANCOUVER ----------
Wolosiuk, R.A., Hertig, C.M., Busconi, L. Activation of spinach chloroplast NADP-linked glyceraldehyde-3-phosphate dehydrogenase by concerted hysteresis. Arch. Biochem. Biophys. 1986;246(1):1-8.
http://dx.doi.org/10.1016/0003-9861(86)90443-1