1988
DOI: 10.1016/s0009-9120(88)80006-7
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Lactate dehydrogenase isolated from human liver mitochondria: Its purification and partial biochemical characterization

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Cited by 10 publications
(6 citation statements)
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“…The latter finding can likely be attributed to the concurrent presence of different isoforms of LDH and MDH. For example, activity of LDH in mitochondria has been reported before [33] and since MDH1 and its mitochondrial isoform MHD2 exhibit the same substrate specificity, the acquired enzyme activity profile presumably reflects the activities of both isoforms. Altogether, our data support the idea that small portions of LDHA and MHD1 are indeed associated with human peroxisomes.…”
Section: Resultsmentioning
confidence: 87%
“…The latter finding can likely be attributed to the concurrent presence of different isoforms of LDH and MDH. For example, activity of LDH in mitochondria has been reported before [33] and since MDH1 and its mitochondrial isoform MHD2 exhibit the same substrate specificity, the acquired enzyme activity profile presumably reflects the activities of both isoforms. Altogether, our data support the idea that small portions of LDHA and MHD1 are indeed associated with human peroxisomes.…”
Section: Resultsmentioning
confidence: 87%
“…236 He/Bremme/Kallner/Blomback LDH in Preeclampsia Other earlier reports asserted that the increase in LDH was associated with liver cell damage [3-6, 8, 9], since elevated ALT and AST concentrations were observed in preeclamptic women with high LDH activity. Some re searchers isolated LDH-5 which is one of the subunit compositions of LDH from liver tissues [10,12]. They found increased concentrations of LDH-5 in preeclamptic women with liver damage.…”
Section: Discussionmentioning
confidence: 99%
“…Therefore, significantly higher activities of these enzymes in PGE1 rabbits compared to IP and AD animals indicated less effective amelioration of liver IRI with PGE1 preconditioning in comparison with IP and AD. While ALT is localized solely in the cellular cytoplasm, AST and LDH are both cytosolic and mitochondrial enzymes (11,12). Hence, considering the significantly higher LDH serum activity in the IP group compared to the AD group, this would suggest a greater hepatocellular damage, including the release of both cytosolic and mitochondrial LDH by mitochondria in IP animals, i.e.…”
Section: Resultsmentioning
confidence: 99%