Bibliographic Citation
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Title | Isolation of chloroplastic phosphoglycerate kinase |
Creator/Author | Macioszek, J. ; Anderson, L.E. (Univ. of Illinois, Chicago (USA)) ; Anderson, J.B. (Pennsylvania State Univ., University Park (USA)) |
Publication Date | 1990 Sep 01 |
OSTI Identifier | OSTI ID: 5857412 |
Other Number(s) | ISSN0032-0889; CODEN: PLPHA |
Resource Type | Journal Article |
Resource Relation | Plant Physiology ; Vol/Issue: 94:1; DOE Project |
Subject | 550500 -- Metabolism; PHOSPHOTRANSFERASES-- BIOCHEMICAL REACTION KINETICS; CHLOROPLASTS;PISUM;PYRIDINES |
Related Subject | AZINES;CELL CONSTITUENTS;ENZYMES;HETEROCYCLIC COMPOUNDS;KINETICS;LEGUMINOSAE;MAGNOLIOPHYTA;MAGNOLIOPSIDA;ORGANIC COMPOUNDS;ORGANIC NITROGEN COMPOUNDS;PHOSPHORUS-GROUP TRANSFERASES;PLANTS;REACTION KINETICS;TRANSFERASES |
Description/Abstract | We report here a method for the isolation of high specific activity phosphoglycerate kinase (EC 2.7.2.3) from chloroplasts.^The enzyme has been purified over 200-fold from pea (Pisum sativum L.) stromal extracts to apparent homogeneity with 23% recovery.^Negative cooperativity is observed with the two enzyme phosphoglycerate kinase/glyceraldehyde-3-P dehydrogenase (EC 1.2.1.13) couple restored from the purified enzymes when NADPH is the reducing pyridine nucleotide, consistent with earlier results obtained with crude chloroplastic extracts.^Michaelis Menten kinetics are observed when 3-phosphoglycerate is held constant and phosphoglycerate kinase is varied, which suggests that phosphoglycerate kinase-bound 1,3-bisphosphoglycerate may be the preferred substrate for glyceraldehyde-3-P dehydrogenase in the chloroplast. |
Country of Publication | United States |
Language | English |
Format | Pages: 291-296 |
System Entry Date | 2001 May 13 |
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