The complete amino acid sequence of the mitochondrial asparate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from human heart has been determined based mainly on analysis of peptides obtained by digestion with trypsin and by chemical cleavage with cyanogen bromide. Comparison of the sequence with those of the isotopic isoenzymes from pig, rat and chicken showed 27, 29 and 55 differences, respectively, out of a total of 401 amino acid residues. Evidence for structural microheterogeneity at position 317 has also been obtained.
The primary structure of mitochondrial aspartate aminotrasferase from human heart / F., Martini; Angelaccio, Sebastiana; Barra, Donatella; Pascarella, Stefano; Maras, Bruno; S., Doonan; Bossa, Francesco. - In: BIOCHIMICA ET BIOPHYSICA ACTA. - ISSN 0006-3002. - 832:(1985), pp. 46-51. [10.1016/0167-4838(85)90172-4]
The primary structure of mitochondrial aspartate aminotrasferase from human heart
ANGELACCIO, Sebastiana;BARRA, Donatella;PASCARELLA, Stefano;MARAS, Bruno;BOSSA, Francesco
1985
Abstract
The complete amino acid sequence of the mitochondrial asparate aminotransferase (L-aspartate:2-oxoglutarate aminotransferase, EC 2.6.1.1) from human heart has been determined based mainly on analysis of peptides obtained by digestion with trypsin and by chemical cleavage with cyanogen bromide. Comparison of the sequence with those of the isotopic isoenzymes from pig, rat and chicken showed 27, 29 and 55 differences, respectively, out of a total of 401 amino acid residues. Evidence for structural microheterogeneity at position 317 has also been obtained.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
