title: Primary structure of rat liver L-threonine deaminase.
abstract: The primary structure of rat liver L-threonine deaminase has been studied utilizing a highly purified preparation (S.A. = 940 U/mg protein) obtained from Wistar male rats. These data have been compared with the predicted sequences obtained by other Authors, showing a considerable concordance with the Noda's prediction and difference with the Ogawa's results. The FAB-MS analysis has demonstrated the presence of an acetyl group as blocking agent on the N-terminal alanine.
authors.affiliation: Istituto di Chimica Biologica, Università, Siena.
authors.forename: R
authors.initials: R
authors.lastname: Leoncini
authors.forename: A
authors.initials: A
authors.lastname: Henschen
authors.forename: K
authors.initials: K
authors.lastname: Krieglstein
authors.forename: J
authors.initials: J
authors.lastname: Calvete
authors.forename: R
authors.initials: R
authors.lastname: Pagani
authors.forename: E
authors.initials: E
authors.lastname: Marinello
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D008099:Liver / Q000201:enzymology*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000032:analysis; D051381:Rats; D011919:Rats, Inbred Strains; D013913:Threonine Dehydratase / Q000737:chemistry*
chemical_list: D010446:Peptide Fragments; D013913:Threonine Dehydratase