[Interaction of aspartate aminotransferase with aminooxyalkylcelluloses]

Interaction of aspartate aminotransferase with various aminooxycelluloses capable of reacting with carbonyl compounds to form oximes has been studied with respect to the distance of the H2NO-groups from the polymer matrix. Aminotransferase does not react with aminooxycelluloses, when the amono-oxygroups are located at small distances from the matrix. When these celluloses interact with the enzyme in the presence of the substrate amino acid, we manage to obtain the amino-form of amino-transferase containing no pyridoxylidine form quantitatively. The cellulose with the H2NO-groups located at considerable distances from the polysaccharide matrix, form the "aminotransferase oxime--aminooxycellulose" complex, which is subsequently split either to a choloenzyme or apoenzyme of PLP and aminooxycellulose, depending on the experimental conditions used. The adsorbents under study may present some interest both in terms of isolation and purfication of pyridoxal enzymes and their effects on enzymatic systems, which contain carbonylic compounds.