Malate dehydrogenase. XI. Absence of tryptophan in porcine heart mitochondrial enzyme

N. L. Eberhardt, R. G. Wolfe

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Native and guanidine hydrochloride-denatured pig heart mitochondrial malate dehydrogenase have fluorescence and phosphorescence emission spectra resembling tyrosine but not that of tryptophan. Furthermore, amino acid analysis of acid and alkaline hydrolysates of the pure enzyme, designed to detect 0.15 tryptophan residues or more per subunit, failed to show detectable quantities. It is confirmed that the enzyme lacks tryptophan and this amino acid can have no function in the catalytic mechanism.

Original languageEnglish (US)
Pages (from-to)151-155
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume160
Issue number1
DOIs
StatePublished - 1974
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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