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  • Title: Clinical significance and partial biochemical characterization of lactate dehydrogenase isoenzyme 6.
    Author: Ketchum CH, Robinson CA, Hall LM, Grizzle WE, Maclaren NK, Riley WJ, Trost C.
    Journal: Clin Chem; 1984 Jan; 30(1):46-9. PubMed ID: 6690151.
    Abstract:
    We report nine patients with a sixth band, migrating cathodic to lactate dehydrogenase 5, appearing on routine electrophoresis for serum lactate dehydrogenase (LD, EC 1.1.1.27). Eight of these patients died during their hospitalization. Acidosis, hypotension, and sepsis were the common clinical conditions preceding the band's appearance. In several cases the band appeared transiently. We examined tissue samples from two of the cases, finding LD-6 in liver and skeletal muscle but not in heart. In randomly selected autopsy tissues, LD-6 was detected consistently in liver and skeletal muscle, sometimes in spleen, kidney, and adrenal tissue, but never in heart. Biochemical studies indicate that the LD-6 isoenzyme is not an artifact or an immunoglobulin complex, is larger than the other LD isoenzymes, contains an M-subunit but not an H-subunit, has an isoelectric point in the pH range of 9.0-9.6, and is more heat stable than LD-5.
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