THE ROLE OF THIOL GROUPS IN THE EXPRESSION OF THE ACTIVITY OF ARGINASE I AND II ISOENZYMES

There are some aspects of the proteins «self-organization» that are not well studied, understanding the relationship between conformational folding linked with the formation of a disulfide bond is important and challenging both from a biophysical and a biochemical perspectives. Studies have attempted to elucidate the role of thiol groups in the maintenance of native conformation and activity of the arginase I and II with a different organ origin. It was identified that depending on the stage of enzyme reactivation and the stability of the conformational state of the formed oligomers, the para-chloromercuribenzoate affects the «self-organised» oligomers in different ways.