FURTHER-STUDIES ON THERMAL-DENATURATION OF PYRUVATE-DEHYDROGENASE COMPLEX FROM BACILLUS-STEAROTHERMOPHILUS

Thermally induced changes in pyruvate dehydrogenase complex (PDC) from B. stearothermophilus were examined mainly at temperatures from 60 de grees to 70 degrees C. Accompanied by inactivation of pyruvate decarbo xylase, light scattering decreased, and ANS fluorescence increased. Th ese changes including the inactivation were approximately first-order reactions, and the values of rate constants were greatly dependent on temperature. Chromatographic studies showed that any polypeptides were in associated forms and that final products were aggregates (>230S) a nd an assembly (48S) smaller than PDC. Th aggregates and assembly were rich in decarboxylase and lipoate acetyltransferase, respectively. It was suggested that, during the thermal denaturation, a decarboxylase was dissociated from PDC and immediately involved in aggregates.