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Characterization of NAD-dependent malate dehydrogenases from spinach leaves
dc.creator | Cvetic, T. | |
dc.creator | Veljović-Jovanović, Sonja | |
dc.creator | Vučinić, Željko | |
dc.date.accessioned | 2022-04-05T14:14:35Z | |
dc.date.available | 2022-04-05T14:14:35Z | |
dc.date.issued | 2008 | |
dc.identifier.issn | 0033-183X | |
dc.identifier.uri | http://rimsi.imsi.bg.ac.rs/handle/123456789/243 | |
dc.description.abstract | Spinach leaves were used to extract isoforms of NAD-dependent malate dehydrogenase (NAD-MDH) (EC 1.1.1.37), either soluble or bound to microsomal, plasma, or chloroplast envelope membranes. All fractions were subjected to isoelectric focusing analysis, which showed that purified chloroplast envelopes contain an NAD-MDH isoform tightly bound to the membranes, since treatment with 0.5 or 1% Triton X-100 was not able to release the enzyme from the envelopes. In contrast, plasma membranes released an isoform with a pI of 3.5 following treatment with 0.5% Triton X-100. The most abundant soluble leaf isoform had a pI of 9, while the chloroplast stroma contained an isoform with a pI of 5.3. Kinetic analysis of oxaloacetate (OAA)-dependent NADH oxidation in different fractions gave different K-m values for both substrates, the envelope- and plasma membrane-bound NAD-MDH exhibiting the highest affinities for OAA. Leaf plasma membrane-bound MDH exhibited a high capacity for both reaction directions (malate oxidation and OAA reduction), while the two chloroplast isoforms (stromal and envelope-bound) preferentially reduced OAA. Our results indicate that the chloroplast envelope contains a specifically attached NAD-MDH isoform that could provide direct coupling between chloroplast and cytosol adenylate pools. | en |
dc.publisher | Springer Wien, Wien | |
dc.rights | restrictedAccess | |
dc.source | Protoplasma | |
dc.subject | Spinacia oleracea | en |
dc.subject | plasma membrane | en |
dc.subject | NAD-dependent malate dehydrogenase | en |
dc.subject | chloroplast envelope membrane | en |
dc.title | Characterization of NAD-dependent malate dehydrogenases from spinach leaves | en |
dc.type | article | |
dc.rights.license | ARR | |
dc.citation.epage | 253 | |
dc.citation.issue | 3-4 | |
dc.citation.other | 232(3-4): 247-253 | |
dc.citation.rank | M22 | |
dc.citation.spage | 247 | |
dc.citation.volume | 232 | |
dc.identifier.doi | 10.1007/s00709-007-0282-7 | |
dc.identifier.pmid | 18239847 | |
dc.identifier.scopus | 2-s2.0-43149091453 | |
dc.identifier.wos | 000256803900013 | |
dc.type.version | publishedVersion |