Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions
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 stimulat...
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todo:paper_00039861_v279_n1_p70_Wolosiuk2023-10-03T13:57:00Z Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions Wolosiuk, R.A. Stein, M. 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 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. Fil:Wolosiuk, R.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Stein, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00039861_v279_n1_p70_Wolosiuk |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 Wolosiuk, R.A. Stein, M. Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| topic_facet |
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 |
| description |
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. |
| format |
JOUR |
| author |
Wolosiuk, R.A. Stein, M. |
| author_facet |
Wolosiuk, R.A. Stein, M. |
| author_sort |
Wolosiuk, R.A. |
| title |
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| title_short |
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| title_full |
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| title_fullStr |
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| title_full_unstemmed |
Modulation of spinach chloroplast NADP-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| title_sort |
modulation of spinach chloroplast nadp-glyceraldehyde-3-phosphate dehydrogenase by chaotropic anions |
| url |
http://hdl.handle.net/20.500.12110/paper_00039861_v279_n1_p70_Wolosiuk |
| work_keys_str_mv |
AT wolosiukra modulationofspinachchloroplastnadpglyceraldehyde3phosphatedehydrogenasebychaotropicanions AT steinm modulationofspinachchloroplastnadpglyceraldehyde3phosphatedehydrogenasebychaotropicanions |
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1807318027917590528 |