Clinical significance and partial biochemical characterization of lactate dehydrogenase isoenzyme 6.

1 January 1984

journal article
research article
Published by Oxford University Press (OUP) in Clinical Chemistry

Vol. 30 (1) , 46-49
https://doi.org/10.1093/clinchem/30.1.46

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.

This publication has 3 references indexed in Scilit:

CIRCULATING IGG-LD COMPLEX, DISSOCIABLE BY ADDITION OF NAD+
1982
Macromolecular Lactic Acid Dehydrogenase
Annals of Internal Medicine, 1974
BIOLOGICAL APPLICATIONS OF LACTIC DEHYDROGENASE ISOZYMES: CERTAIN METHODOLOGICAL CONSIDERATIONS*
Annals of the New York Academy of Sciences, 1964