Abstract
The dissociative condition of Asp-hemolysin, a protein toxin purified from Aspergillus fumigatus, into subunits was investigated.
The extent of dissociation by sodium dodecyl sulfate (SDS) as examined by slab-gel electrophoresis (SDS-PAGE) depended on SDS concentration, pH, and reaction time. Concentration of slab-gel was also an important factor in resolving the resultant subunits. Asp-hemolysin protein was found to dissociate into three subunits, (A), (B), and (C), when incubated in the best dissociative condition of 1% SDS, and pH 8.0 for 2hr. The molecular weights of subunits isolated by SDS-PAGE were A: 15500, B: 12000 and C: 8000 in a molar ratio of 2:1:2, respectively.
Three protein bands were detected by Toyopearl HW-50 column chromatography in the presence of 1% SDS and 20mM 2-mercaptoethanol.
One hundred micrograms of any of the three subunits had no hemolytic activity by itself.
