Collect. Czech. Chem. Commun. 1989, 54, 2528-2541

Immobilization of ribonucleotide reductase from Streptomyces aureofaciens

Peter Halickýa, Marta Kollárováa, Pavol Koisb and Ján Zelinkaa

a Department of Biochemistry, Komenský University, 842 15 Bratislava
b Institute of Biochemistry and Biotechnology, Komenský University, 842 15 Bratislava


Ribonucleotide reductase from Streptomyces aureofaciens (E.C.1.17.4.) has been isolated. The effects of concentration of substrate, effector, coenzyme, reductant, pH, and ionic strength upon the activity of this enzyme have been studied and the data obtained by research have been completed. Based on some properties of this enzyme, we have chosen a proper hydrophobic carrier-Trityl-agarose for immobilization. It has been found out that the properties of the immobilized enzyme are significantly different from those of the free enzyme. Principal differences are in the loss of the effector dependence of the immobilized enzyme and in a significant increase of its stability.