Answer
Yes, the results support the hypothesis that phenylalanine is an allosteric regulator of phenylalanine hydroxylase (PAH) because a new, smaller protein product is produced after exposure of PAH to trypsin in the presence of phenylalanine.
According to the electrophoretic data, PAH undergoes a conformational change when exposed to phenylalanine because these changes allow the digestion of PAH by trypsin in the presence of phenylalanine.
Work Step by Step
Gel electrophoresis separates molecules based on their size. When run in a gel, molecules move different distances based on both these factors.
The presence of multiple bands, as in the case of trypsin (+) and phenylalanine (+), indicates that trypsin has indeed cleaved PAH, which is otherwise present as a single band in phenylalanine (-) and trypsin (-).
