Sulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5'-dithiobis (2-nitrobenzoic acid). From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other sources
Primary structure of aspartate aminotrasferase from horse hearth and comparison with that of other homotopic and heterotopic isoenzymes / F., Martini; Angelaccio, Sebastiana; Barra, Donatella; S., Doonan; Bossa, Francesco. - In: COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY. B, COMPARATIVE BIOCHEMISTRY. - ISSN 0305-0491. - 73B:(1983), pp. 483-487.
Primary structure of aspartate aminotrasferase from horse hearth and comparison with that of other homotopic and heterotopic isoenzymes
ANGELACCIO, Sebastiana;BARRA, Donatella;BOSSA, Francesco
1983
Abstract
Sulphydryl groups of mitochondrial aspartate aminotransferase from horse heart were titrated with 5,5'-dithiobis (2-nitrobenzoic acid). From analysis of peptic peptides, 378 amino acid residues (94.3% of the total) in the protein were identified. The results of amino acid sequence analysis are compared with those of cytosolic and mitochondrial aspartate aminotransferases from other sourcesI documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
