For the first time an interaction between aspartate transaminase (EC 2.6.1.1.) from chicken heart cytosol and the substrates and their analogues has been investigated by means of circular dichroism and absorption spectra (at pH 5,0-8,0 range). The asymmetry factor of the native enzyme and the enzymes--substrate intermediates was found. The results obtained were explained in terms of changes of the enzyme's active site conformation.
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