Source:http://linkedlifedata.com/resource/pubmed/id/16666441
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| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2010-6-29
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| pubmed:abstractText |
Protoplasts purified from pea (Pisum sativum L.) leaves were lysed and fractionated to assess the subcellular distribution of NADPH-dependent hydroxypyruvate reductase (NADPH-HPR) activity. Rate-zonal centrifugation and sucrose-gradient experiments demonstrated that most (about 70%) of the NADPH-HPR activity was located in the supernatant or cytosol fraction. Detectable, but relatively minor activities were associated with the chloroplast fraction (up to 10% on a chlorophyll basis when compared to the lysate) and with peroxisomes. The minor NADPH-HPR activity in the peroxisomes could be fully accounted for by the secondary NADPH-dependent activity of NADH-dependent HPR. The subcellular distribution of NADPH-HPR followed closely that previously determined for NADPH-dependent glyoxylate reductase (NADPH-GR), an enzyme localized predominantly in the cytosol of pea leaf protoplasts (CV Givan et al. 1988 J Plant Physiol 132: 593-599). Low activities of both NADPH-HPR and NADPH-GR were also found in purified chloroplasts prepared by mechanical homogenization of Pisum and Spinacia leaves. In pea and spinach chloroplasts, rates of both NADPH-HPR and NADPH-GR were lower than the activity of the NADH-dependent GR. The results are discussed in relation to a possible role for NADPH-HPR in the oxidative carbon pathway of photorespiration. Both NADPH-HPR and the GRs could function as auxiliary reactions to photorespiration, utilizing hydroxypyruvate and/or glyoxylate ;leaked' or otherwise exported from peroxisomes. NADPH-HPR function might be especially significant under conditions of limiting NADH supply to peroxisomes, with extraperoxisomal reduced pyridine nucleotide acting as the reductant.
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| pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-14010085,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16654194,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16658629,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16658807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16660703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16661695,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16661892,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16663015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16663075,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16664100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-16665491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-2981505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-3080957,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-3281657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-3548703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-3663185,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-4294897,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16666441-4394164
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:status |
PubMed-not-MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0032-0889
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
88
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1182-5
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| pubmed:dateRevised |
2010-9-15
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| pubmed:year |
1988
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| pubmed:articleTitle |
Subcellular Location of NADPH-Dependent Hydroxypyruvate Reductase Activity in Leaf Protoplasts of Pisum sativum L. and Its Role in Photorespiratory Metabolism.
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| pubmed:affiliation |
Department of Biology, Ridley Building, University of Newcastle upon Tyne, England, U.K.
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| pubmed:publicationType |
Journal Article
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