Primary structure of rat liver L-threonine deaminase.
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.
Leoncini
R
R
Istituto di Chimica Biologica, Università, Siena.
Henschen
A
A
Krieglstein
K
K
Calvete
J
J
Pagani
R
R
Marinello
E
E
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*
D010446:Peptide Fragments; D013913:Threonine Dehydratase