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 language | English |
|---|---|
| Pages (from-to) | 507-509 |
| Number of pages | 3 |
| Journal | Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular Biology |
| Volume | 82 |
| Issue number | 3 |
| DOIs | |
| State | Published - 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
- Biochemistry
- Physiology
- Molecular Biology