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the level of L-lactate dehydrogenase B are specifically increased in non-small cell lung cancer
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LDH2
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lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
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embryonic membrane of oncosphere
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isolated milk epithelial cell
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cerebellar
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lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
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fat-free milk, or 2% fat milk
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primary non-small cell lung cancer cell line
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brain metastatic subline of NCI-H226. L-lactate dehydrogenase B is significantly up-regulated in the conditional medium of NCI-H226Br cells
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activities of both H- and M-isoforms of LDH are high but neurons show a dominance of H-isoform activity
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lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
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patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-3, LDH-2 and LDH-1
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lactate dehydrogenase-B is silenced by promoter hypermethylation in human prostate cancer
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patients with tubercular pyothorax show highest levels in LDH-5 followed by LDH-4, LDH-2, LDH-3 and LDH-1. In LDH-5 and LDH-4 nearly 4- and 5folds increase in patients
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muscle
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contains a skeletal muscle type and heart type mixed heterotetrameric enzyme, H2M2
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normal and malignant human breast tissues
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normal and malignant human breast tissues. The enzyme is highly expressed in breast
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endometrial and ovarian
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differential expressions of LDH isozymes in different types of tumors
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differential expressions of LDH isozymes in different types of tumors
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FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked
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FBP-activated L-nLDH activity is constantly very significant throughout the growth period, even when lactate is consumed in the stationary phase of respiration. During the lactate utilization period, L-nLDH activity is regulated by some factors and the pyruvate reduction activity is completely inhibited or masked
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steady-state growth at pH 7 and pH 5
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steady-state growth at pH 7 and pH 5
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from muscle
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in patients with tubercular pyothorax, decrease in heart specific aerobic LDH-1 (6fold), LDH-2 (2fold) and LDH-3 (1.5fold)
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H-type isozyme
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H-type isozyme
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heart-type isozyme
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contains a heart type homotetrameric enzyme, H4
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tail muscle
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significant rise in the level of muscle specific anaerobic LDH-5 and LDH-4 in patients with tubercular pyothorax
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M-type isozyme
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M-type isozyme
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muscle isozyme
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isoenzyme LDH-A4
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muscle isozyme
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muscle-type isozyme, i.e. M4 isoform
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contains a skeletal muscle type homotetrameric enzyme, M4
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isoenzyme LDH-B4 and LDH-A2B2
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additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
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structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
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structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
LDH is stage specifically transcribed in Eimeria, but its presence at the protein level remains constant during different life-cycle stages
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additional information
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LDH is stage specifically transcribed in Eimeria, but its presence at the protein level remains constant during different life-cycle stages
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additional information
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tissue-specific expression analysis, overview
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additional information
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homo- and heterotetrameric isozymes with tissue-specific expression
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additional information
serum LDH is commonly increases in patients with hematopoietic malignancies, such as Hodgkin's lymphoma, non-Hodgkin's lymphoma, or multiplemyeloma
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additional information
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in satellite gliocytes, activities of both H- and M-isoforms of LDH are high, dominance of M-isoform activity
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additional information
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type-I isolate, e.g. strain NRRL 395, accumulating primarily lactic acid when grown in the presence of a fermentable carbon source and containing two LDH genes, ldhA and ldhB, and type-II isolates, e.g. strain 99-880, synthesizing predominantly fumaric acid and having only an ldhB gene
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additional information
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metabolic adaptation of Staphylococcus aureus to nitrosative stress, overview
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additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
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additional information
in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
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additional information
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in somatic cells, LDH forms homotetramers and heterotetramers that are encoded by two different genes: LDHA (skeletal muscle type, M) and LDHB (heart type, H)
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additional information
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surface of the tegument in adults. Is absent from internal tissues
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additional information
structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
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structural features for structural stability, comparison to enzymes from other species in extreme environments
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additional information
LDH1 is absent from bradyzoites
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additional information
LDH1 is absent from bradyzoites
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additional information
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LDH1 is absent from bradyzoites
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additional information
LDH2 is absent from tachyzoites
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additional information
LDH2 is absent from tachyzoites
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additional information
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LDH2 is absent from tachyzoites
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