| Literature DB >> 7599526 |
L E Anderson1, I M Goldhaber-Gordon, D Li, X Y Tang, M Xiang, N Prakash.
Abstract
Apparent physical interaction between pea chloroplast (Pisum sativum L.) glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.13) and aldolase (EC 4.1.2.13) is seen in phase-partitioning, fluorescent-anisotropy and isoelectric-focusing experiments. Similarly, results obtained in phase-partitioning and isoelectric-focusing experiments indicate physical interaction between aldolase and triose-phosphate isomerase (EC 5.3.1.1). Kinetic experiments suggest that both aldolase-bound glyceraldehyde-3-phosphate can act as substrate for glyceraldehyde-3-phosphate dehydrogenase. These results are consistent with the notion that there is interaction between these three enzymes both during photosynthetic CO2 fixation and during glycolysis in the chloroplast.Entities:
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Year: 1995 PMID: 7599526 DOI: 10.1007/BF00201381
Source DB: PubMed Journal: Planta ISSN: 0032-0935 Impact factor: 4.116