OPTICAL-ACTIVITY OF ASPARTATE-AMINOTRANSFERASE

The absorption and circular dichroism spectra of aspartate aminotransf erase (EC 2.6.1.1) from chicken heart cytosol and the complex of the e nzyme with erythro-3-hydroxyaspartate were recorded in potassium phosp hate buffer at pH 4.3-9.5. The anisotropy factors of the free enzyme a nd its complex were determined. On the basis of the changes of the ani sotropy factors, the subunits of aspartate aminotransferase are sugges ted to have different optical activities.