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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1995-8-7
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pubmed:databankReference |
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/D13513,
http://linkedlifedata.com/resource/pubmed/xref/GENBANK/X69969,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P00883,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P00884,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P04075,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P05062,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P05064,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P05065,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P07341,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P07752,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P07764,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P08440,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P09117,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P09972,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P14223,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P16096,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P17784,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P22197,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/P29356,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/Q01516,
http://linkedlifedata.com/resource/pubmed/xref/SWISSPROT/Q01517
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
B
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:issn |
0032-0935
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
196
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7599526-Amino Acid Sequence,
pubmed-meshheading:7599526-Animals,
pubmed-meshheading:7599526-Chloroplasts,
pubmed-meshheading:7599526-Chromatography, DEAE-Cellulose,
pubmed-meshheading:7599526-Chromatography, Gel,
pubmed-meshheading:7599526-Countercurrent Distribution,
pubmed-meshheading:7599526-Fructose-Bisphosphate Aldolase,
pubmed-meshheading:7599526-Glyceraldehyde-3-Phosphate Dehydrogenases,
pubmed-meshheading:7599526-Humans,
pubmed-meshheading:7599526-Kinetics,
pubmed-meshheading:7599526-Molecular Sequence Data,
pubmed-meshheading:7599526-Peas,
pubmed-meshheading:7599526-Sequence Homology, Amino Acid,
pubmed-meshheading:7599526-Triose-Phosphate Isomerase
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pubmed:year |
1995
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pubmed:articleTitle |
Enzyme-enzyme interaction in the chloroplast: glyceraldehyde-3-phosphate dehydrogenase, triose phosphate isomerase and aldolase.
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pubmed:affiliation |
Department of Biological Sciences, University of Illinois at Chicago 60607-7060, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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