[Glyceraldehyde-3-phosphate dehydrogenase stabilization by the introduction of intersubunit linkages]

To work out methods of synthesis of stabilized enzymatic preparations for clinical application, subunit enzyme glyceraldehyde-3-phosphatedehydrogenase was treated with bifunctional reagents--aliphatic diacids, activated by water-soluble carbodiimide. Gel-electrophoresis in the presence of natrium dodecyl sulfate showed the presence of a linkage between the subunits. The maximal thermostability was observed in the preparations treated with amber and glutaric acid. These preparations also contained the maximal amount of the enzymatic fraction, which did not dissociate into subunits. The data of EPR-spectroscopy showed that the preparations of the enzyme with the introduced intersubunit linkages had a lowered molecular mobility.