Paramax triglycerides reagent: interference from high L-lactate and lactate dehydrogenase
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منابع مشابه
The mitochondrial L-lactate dehydrogenase affair
The existence of a mitochondrial L-lactate dehydrogenase (m-L-LDH) suggested by Dianzani (1951), was shown by Baba and Sharma (1971) with the enzyme located in the mitochondrial matrix; later Brooks et al. (1999) proposed the intracellular lactate shuttle and in the third millennium the existence of m-L-LDH was definitively been confirmed in mammalian, plant and yeast mitochondria as reviewed b...
متن کاملInducible Membrane-bound L-Lactate Dehydrogenase from Escherichia coZi
Membrane-bound L-lactate dehydrogenase was solubilized from the membranes ofEscherichia coli and purified to homogeneity using conventional procedures. The enzyme had a pH optimum of 8 to 9 and was specific for L-lactate. Its apparent K, for L-lactate and maximal velocity were 1.2 x lo-’ M and 31 pmol of tetrazolium dye reducedlminlmg of protein, respectively. It had a polypeptide molecular wei...
متن کاملCharacterization of the L-Lactate Dehydrogenase from Aggregatibacter actinomycetemcomitans
Aggregatibacter actinomycetemcomitans is a Gram-negative opportunistic pathogen and the proposed causative agent of localized aggressive periodontitis. A. actinomycetemcomitans is found exclusively in the mammalian oral cavity in the space between the gums and the teeth known as the gingival crevice. Many bacterial species reside in this environment where competition for carbon is high. A. acti...
متن کاملLACTATE DEHYDROGENASE Elevation ofserum lactate dehydrogenasecommences
Heart tissue injury may release cardiac enzymes into the circulation and elevate serum enzyme levels (LaDue, Wroblewski, and Karmen, 1954). Many enzymes become raised, but three enzymesaspartate aminotransferase (EC 2.6.1.1), creatine kinase (EC 2.7.3.2), and lactate dehydrogenase (EC 1.1.1.27)-have proved of particular diagnostic value. In addition, determination of lactate dehydrogenase isoen...
متن کاملNAD-Independent L-Lactate Dehydrogenase Is Required for L-Lactate Utilization in Pseudomonas stutzeri SDM
BACKGROUND Various Pseudomonas strains can use L-lactate as their sole carbon source for growth. However, the L-lactate-utilizing enzymes in Pseudomonas have never been identified and further studied. METHODOLOGY/PRINCIPAL FINDINGS An NAD-independent L-lactate dehydrogenase (L-iLDH) was purified from the membrane fraction of Pseudomonas stutzeri SDM. The enzyme catalyzes the oxidation of L-la...
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ژورنال
عنوان ژورنال: Clinical Chemistry
سال: 1996
ISSN: 0009-9147,1530-8561
DOI: 10.1093/clinchem/42.5.778