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Serum from a patient with hepatocellular carcinoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), LDH-1ex, that on electrophoresis on 10-g/L agarose gel migrated anodally to the LDH-1 band. This isoenzyme was partly purified by ultrafiltration and preparative electrophoresis. Gel chromatography and sodium dodecyl sulfate/polyacrylamide gel electrophoresis studies of the resulting LDH-1ex preparation suggested that this isoenzyme is probably a tetramer made up of four single polypeptide chains (monomers), each having a molecular mass of about 32,000 Da. LDH-1ex was heat stable and reacted more readily with 2-hydroxybutyrate than did the slower migrating LDH-4 and LDH-5 isoenzymes. LDH-1ex showed no activity when lactate was omitted from the substrate solution or replaced by ethanol.
D L Kalpaxis, and
E E Giannoulaki
August 1983,
Clinical chemistry,
D L Kalpaxis, and
E E Giannoulaki
November 1990,
Clinical chemistry,
D L Kalpaxis, and
E E Giannoulaki
November 1992,
Clinical chemistry,
D L Kalpaxis, and
E E Giannoulaki
February 1985,
Clinical chemistry,
D L Kalpaxis, and
E E Giannoulaki
May 1976,
Clinica chimica acta; international journal of clinical chemistry,
D L Kalpaxis, and
E E Giannoulaki
July 1984,
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D L Kalpaxis, and
E E Giannoulaki
March 1999,
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D L Kalpaxis, and
E E Giannoulaki
December 1983,
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D L Kalpaxis, and
E E Giannoulaki
June 1970,
The Journal of urology,
D L Kalpaxis, and
E E Giannoulaki
February 1984,
Clinical chemistry,
