1. 1. Lactate dehydrogenase was purified to homogeneity from the chilopod Scolopendra cingulata. 2. 2. The enzyme has the usual molecular weight of approximately 150,000 and exists as a tetramer. It is l(+)lactate specific and some lines of evidence ascribe the molecule to the A-class (muscle-type of vertebrates). 3. 3. Surprisingly it displays Kcat values for both substrates pyruvate and lactate which are about two orders of magnitude lower than those known for other lactate dehydrogenases. 4. 4. Additionally, both Km for lactate and Kcat/Km for pyruvate are independent from assay temperature. 5. 5. The most striking feature of this enzyme, however, is its stability, as it still retains activity either after incubation at 90°C or in the presence of urea concentrations as high as 7.5 M.
|Number of pages||6|
|Journal||Comparative Biochemistry and Physiology - B Biochemistry and Molecular Biology|
|Publication status||Published - 1990|
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