Structural analysis of adult and larval isozymes of sn-glycerol-3-phosphate dehydrogenase of Drosophila melanogaster.

D. W. Niesel, Y. C. Pan, G. C. Bewley, F. B. Armstrong, S. S. Li

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

Compositional analysis of the soluble tryptic peptides representing about 70% of the 293 residues of sn-glycerol-3-phosphate dehydrogenase in Drosophila melanogaster reveals a single peptide difference between the sn-glycerol-3-phosphate dehydrogenase adult (GPDHF-1) and larval (GPDHF-3) isozymes. This peptide was shown to be the carboxyl terminus by sequence determination and by carboxypeptidase A digestion of the native protein. For GPDHF-1, the sequence of the COOH-terminal tryptic peptide is Asn-His-Pro-Glu-His-Met-Gln-Asn-Leu-COOH, while that of GPDHF-3 is Asn-His-Pro-Glu-His-Met-COOH.

Original languageEnglish (US)
Pages (from-to)979-983
Number of pages5
JournalJournal of Biological Chemistry
Volume257
Issue number2
StatePublished - Jan 25 1982
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Structural analysis of adult and larval isozymes of sn-glycerol-3-phosphate dehydrogenase of Drosophila melanogaster.'. Together they form a unique fingerprint.

Cite this