Optical Activity of Aspartate Aminotransferase

V. M. Kochkina¹

¹Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, ul. Vavilova 32, 117984 Russia; fax: (7-095) 135-14-05.

Submitted July 7, 1996; revision submitted December 18, 1996.

The absorption and circular dichroism spectra of aspartate aminotransferase (EC 2.6.1.1) from chicken heart cytosol and the complex of the enzyme with erythro-3-hydroxyaspartate were recorded in potassium phosphate buffer at pH 4.3-9.5. The anisotropy factors of the free enzyme and its complex were determined. On the basis of the changes of the anisotropy factors, the subunits of aspartate aminotransferase are suggested to have different optical activities.

KEY WORDS: aspartate aminotransferase, absorption spectra, circular dichroism, anisotropy factor.

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