[Cytosol aspartate aminotransferase from the chicken heart: three-dimensional structure at 2.8 angstroms resolution and the characteristic conformation of various enzyme forms].

The spatial structure of cytosolic chicken aspartate aminotransferase (AAT) has been determined by X-ray crystallographic analysis at 2.8 A resolution. AAT consists of two chemically identical subunits.

[Primary structure of the cytoplasmic aspartate aminotransferases from the swine myocardium. Isolation, purification and characteristics of the peptides from cyanogen bromide cleavage].

Cytoplasmic aspartate aminotransferase from pig heart muscle was cleaved with cyanogen bromide and 8 peptide fragments were isolated. The high tendency of the large peptides for aggregation was overcome only by the utilization of special procedures of the denaturation and acylation of the lysine residues of peptide with citraconic anhydride. Peptides were separated by gel chromatography on sephadex G-50 and G-75 and by ion exchange chromatography on cellulose DE-22 and DE-32 with use of concentrated urea solutions.