Isoenzymic forms of NAD-linked glycerol-3-phosphate dehydrogenase from rabbit brain

Richard Kornbluth, Paula S. Tracy, Thomas P. Fondy

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Two major enzyme forms of cytosolic NAD-linked glycerol-3-phosphate dehydrogenase in rabbit brain have been purified to apparent homogeneity. One major enzyme form designated I6.5 exhibits an iso-electric point at pH 6.5, and is indistinguishable from the major form I6.5 found in other tissues. The other major form, designated I5.9, has an isoelectric point at pH 5.9, and by amino acid analysis is shown to be a true isoenzyme distinct from form I6.5. Form I5.9 appears to be closely related to or identical with the major enzyme characteristic of heart. Neither the brain enzyme form I5.9 nor the major heart isoenzyme are inhibited by antiserum to the muscle enzyme. Because of the high apparent Km for NADH, it is postulated that the brain isoenzyme I5.9 serves to maintain glycolysis when NADH levels rise under relatively anaerobic conditions especially during fetal and neonatal development.

Original languageEnglish (US)
Pages (from-to)273-286
Number of pages14
JournalBBA - Enzymology
Volume568
Issue number2
DOIs
StatePublished - Jun 6 1979

Keywords

  • (Brain)
  • Glycerol-3-phosphate dehydrogenase isoenzyme
  • NAD-linked

ASJC Scopus subject areas

  • Medicine(all)

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