نتایج جستجو برای: lactate dehydrogenase ldh

تعداد نتایج: 94215  

2013
Neal J. Dawson Ryan A. V. Bell Kenneth B. Storey

Lactate dehydrogenase (LDH; E.C. 1.1.1.27) is a crucial enzyme involved in energy metabolism in muscle, facilitating the production of ATP via glycolysis during oxygen deprivation by recycling NAD(+). The present study investigated purified LDH from the muscle of 20 h anoxic and normoxic T. s. elegans, and LDH from anoxic muscle showed a significantly lower (47%) K m for L-lactate and a higher ...

Journal: :Journal of the American College of Cardiology 2011

Journal: :Endocrinology 1997
Diane Nehar Claire Mauduit Fayc Al Boussouar Mohamed Benahmed

By using, as a model, cultured testicular immature Sertoli cells, the action of tumor necrosis factor-alpha (TNF alpha) and the site of action of the cytokine on lactate production were studied. TNF alpha stimulated in a time- and dose-dependent manner (with an ED50 of 0.1 nM) Sertoli cell lactate production. Two major sites involved in TNF alpha action were identified. Firstly, TNF alpha was s...

Journal: :Annals of clinical and laboratory science 2006
Kiyotaka Fujita Hirohisa Sato Fumiko Kameko Fumiko Terasawa Nobuo Okumura Mitsutoshi Sugano Kazuyoshi Yamauchi Masato Maekawa Ikunosuke Sakurabayashi

We discovered a patient with low serum lactate dehydrogenase (LD) activity and an abnormal LD isozyme pattern. We analyzed the patient's LD inhibitor using electrophoresis, affinity chromatography, and immunochemical technologies. The LD activity of the patient's serum was inhibited more strongly at 4 degrees C than at 37 degrees C. The decrease of LD activity was more marked in a mixture of th...

Journal: :Genetics 1987
K M Fukasawa S S Li

The complete sequence of 12,851 nucleotides of the mouse lactate dehydrogenase-A (LDH-A) gene has been determined. It includes eight exons, seven introns, promoter and regulatory regions. The B1 repetitive elements present in intron III and VI are oriented in opposite orientation, and they share 72% sequence homology. The exon-intron organization of mouse LDH-A gene is compared with the organiz...

2015
Khyati K. Dave Narayan S. Punekar Daniel Cullen

Different engineered organisms have been used to produce L-lactate. Poor yields of lactate at low pH and expensive downstream processing remain as bottlenecks. Aspergillus niger is a prolific citrate producer and a remarkably acid tolerant fungus. Neither a functional lactate dehydrogenase (LDH) from nor lactate production by A. niger is reported. Its genome was also investigated for the presen...

Journal: :Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas 1997
V I Lushchak T V Bahnjukova A V Spichenkov

The modification of pyruvate kinase (PK) and lactate dehydrogenase (LDH) activity in foot muscle of the mussel Mytilus galloprovincialis during exposure to air and recovery in water was investigated. In the course of exposure to air, the activity of these enzymes measured at high and low substrate concentrations showed successive increases and decreases. Returning the mussels to water after exp...

2002
Jean Rivoal

Roots of all plants examined so far have the potential for both ethanol and lactate fermentation. A short burst of lactate fermentation usually occurs when plant tissues are transferred from normoxic to anoxic conditions. According to the Davies-Roberts hypothesis, the consequent pH drop both initiates ethanol fermentation and blocks further production of Iadate by inhibiting lactate dehydrogen...

2013
Di Zhao Yue Xiong Qun-Ying Lei Kun-Liang Guan

Upregulation of lactate dehydrogenase A (LDH-A) is commonly observed in many tumor types. Previous studies have revealed LDH-A transcriptional activation by the increased activity of Myc and HIF in human cancers. Is LDH-A regulated by post-translational modifications during tumorigenesis? If so, can such knowledge be used to assist cancer early diagnosis and treatment? Reprogramming of energy m...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2009
Grigory E Pinchuk Dmitry A Rodionov Chen Yang Xiaoqing Li Andrei L Osterman Etienne Dervyn Oleg V Geydebrekht Samantha B Reed Margaret F Romine Frank R Collart James H Scott Jim K Fredrickson Alexander S Beliaev

The ability to use lactate as a sole source of carbon and energy is one of the key metabolic signatures of Shewanellae, a diverse group of dissimilatory metal-reducing bacteria commonly found in aquatic and sedimentary environments. Nonetheless, homology searches failed to recognize orthologs of previously described bacterial d- or l-lactate oxidizing enzymes (Escherichia coli genes dld and lld...

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