Primary structure of the essential thiol peptide from the lactate dehydrogenase C subunit

Thomas E. Wheat*, Erwin Goldberg, E. Margoliash

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

8 Scopus citations

Abstract

Lactate dehydrogenase isozymes are inhibited when mercurial reagents are bound to cysteine-165 although no functional role is ascribed to this residue. Identical tryptic peptides containing this cysteine have been isolated from many LDH isozymes, including both A and B subunits. This report identifies an identical peptide from a third subunit type, C, of mouse. The rigorous conservation of this sequence implies an important functional role for this region of the molecule.

Original languageEnglish (US)
Pages (from-to)1066-1070
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume74
Issue number3
DOIs
StatePublished - Feb 7 1977

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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