Abstract
The low molecular weight, inactive form of pneumococcal amidase called E-amidase showed the full activity and a high molecular mass (> 500 kDa) when the enzyme was incubated with high concentrations of choline followed by the removal of excess choline. Before the removal of choline, the enzyme showed a low molecular mass-material (about 36 kDa) similar to that of the original E-amidase, suggesting that the aggregation of the protein took place upon the removal of choline. Furthermore, the addition of choline to the native C-amidase (active form) which had a high molecular mass (> 500 kDa) caused dissociation to a low molecular mass enzyme (about 36 kDa) in the presence of choline. These dissociated enzymes reaggregated upon the removal of choline.
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