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Abstract:

Neutral salts enhanced the specific activity of chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase (d-glyceraldehyde-3-phosphate:NADP+ oxidoreductase (phosphorylating), EC 1.2.1.13) from spinach leaves. The ordering of the respective anions, according to the concentration for maximal stimulation, yielded the lyotropic (Hofmeister) series [SCN- (0.05 m), ClO4- (0.08 m), Cl3CCO2- (0.24 m), I- (0.35 m), Br- (0.6 m), Cl- (1.0 m)]; the more chaotropic the anion the less its concentration for maximal activation. Neither the NAD-linked activity of the chloroplast enzyme nor glyceraldehyde-3-phosphate dehydrogenases originating from cyanobacteria and rabbit muscle were stimulated by neutral salts. Chaotropic anions also enhanced the catalytic capacity of the chloroplast enzyme at concentrations lower than those required for the activation process. In the presence of 0.12 m NaBr the rate of catalysis was maximum whereas the highest conversion from the inactive to an active form was observed at 0.6 m NaBr. On the other hand, nonstimulatory concentrations of chaotropic anions lowered the concentration of ATP, Pi, and NADPH required for maximum stimulation of the specific activity (concerted hysteresis). On the basis that the enhancement of NADP-glyceraldehyde-3-phosphate dehydrogenase (and other chloroplast enzymes) by chaotropic anions paralleled the effect of organic solvents and reduced thioredoxin, it appeared that the modification of hydrophobic (intramolecular) interactions participates in the mechanism of light-mediated regulation. © 1990.

Registro:

Documento: Artículo
Título:Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions
Autor:Wolosiuk, R.A.; Stein, M.
Filiación:Instituto de Investigaciones Bioquimicas, Fundacion Campomar, FCEN-UBA, Antonio Machado 151, 1405 Buenos Aires, Argentina
Palabras clave:glyceraldehyde 3 phosphate dehydrogenase (NADP)(phosphorylating); nicotinamide adenine dinucleotide phosphate glyceraldehyde 3 phosphate dehydrogenase; unclassified drug; article; enzyme regulation; higher plant; nonhuman; priority journal; spinach; Aldehyde Oxidoreductases; Anions; Bromides; Chloroplasts; Glyceraldehyde-3-Phosphate Dehydrogenases; NADP; Oxidation-Reduction; Plants; Sodium; Support, Non-U.S. Gov't; Cyanobacteria; Embryophyta; Oryctolagus cuniculus; Spinacia oleracea
Año:1990
Volumen:279
Número:1
Página de inicio:70
Página de fin:77
DOI: http://dx.doi.org/10.1016/0003-9861(90)90464-A
Título revista:Archives of Biochemistry and Biophysics
Título revista abreviado:Arch. Biochem. Biophys.
ISSN:00039861
CODEN:ABBIA
CAS:Aldehyde Oxidoreductases, EC 1.2.; Anions; Bromides; Glyceraldehyde-3-Phosphate Dehydrogenases, EC 1.2.1.-; NADP, 53-59-8; sodium bromide, 7647-15-6; Sodium, 7440-23-5
Registro:https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00039861_v279_n1_p70_Wolosiuk

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Citas:

---------- APA ----------
Wolosiuk, R.A. & Stein, M. (1990) . Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions. Archives of Biochemistry and Biophysics, 279(1), 70-77.
http://dx.doi.org/10.1016/0003-9861(90)90464-A
---------- CHICAGO ----------
Wolosiuk, R.A., Stein, M. "Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions" . Archives of Biochemistry and Biophysics 279, no. 1 (1990) : 70-77.
http://dx.doi.org/10.1016/0003-9861(90)90464-A
---------- MLA ----------
Wolosiuk, R.A., Stein, M. "Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions" . Archives of Biochemistry and Biophysics, vol. 279, no. 1, 1990, pp. 70-77.
http://dx.doi.org/10.1016/0003-9861(90)90464-A
---------- VANCOUVER ----------
Wolosiuk, R.A., Stein, M. Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions. Arch. Biochem. Biophys. 1990;279(1):70-77.
http://dx.doi.org/10.1016/0003-9861(90)90464-A