Distribution of a COOH-terminal amino acid extension of liver fructose-1,6-bisphosphatase among rodent species

Judith Rittenhouse, Eviatar Nevo, Frank Marcus

Research output: Contribution to journalArticlepeer-review

Abstract

1. 1. We have recently established from sequence analysis that rat liver fructose-1,6-bisphosphatase contains a 24-26 residue extension beyond the COOH-terminal amino acid of other mammalian fructose-1,6-bisphosphatases that results in an increased subunit molecular weight (Rittenhouse et al. (1983) J. Biol. Chem. 258, 7648-7652). 2. 2. In the present work the distribution of the COOH-terminal extension of fructose-1,6-bisphosphatases was tested by subunit molecular weight analysis of the enzyme immunoprecipitated from liver extracts. 3. 3. Of all rodent species tested, including several Muridae other than Rattus; only the enzyme from animals of the genus Rattus was found to have the extension. Further studies on the distribution of the enzyme extension could provide a simple tool to study the phylogeny of the genus Rattus.

Original languageEnglish
Pages (from-to)507-509
Number of pages3
JournalComparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology
Volume82
Issue number3
DOIs
StatePublished - 1985

Bibliographical note

Funding Information:
Ackno,'ledgernentTsh-is work was supportedb y the National Instituteso f Health (Grant AM 21167)t,h e AncelI-TeicherR esearchFo undationt or Geneticsa nd MolecularE volutiona, nd theI sraelD iscounBt ankC hair of EvolutionaryB iology.W e thankS . Simsonfo r field work.

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry
  • Physiology

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