Partial purification means the enzyme is partially purified, so what happen to other partial of the crude enzyme sample being subjected to this partial purification?
Pure enzyme is normally a single homogenous protein which shows the highest specific activity expressed, let us say, micro moles/mg protein/hour. So the specific activity will be less for an impure (heterogeneous) enzyme mixed with other junk proteins. The other partial is generally lost during the enrichment procedure of the pure form involving many steps from contaminated proteins.
It is a possibility that the yield of the specific protein of interest is 100% (i.e. it is all recovered) but its purity is less than 100% (partial purification). Sometimes, to get higher purity it is necessary to sacrifice yield. For example, you might throw away less pure fractions from the edges of the protein peak eluted from a column and keep the purer fractions from the middle.
Enzyme partial purification: suppose pro-enzyme and coenzyme involved In the activity example dehydrogenase enzyme + coenzyme (NAD or NADH) on purification of enzyme the E.activity will be lost due to lack of NADH on addition the activity is restored.
There are some metalo- enzymes where the specific activity of the enzyme depends on the metal present
So, in some cases partial purification (ammonia sulphate) is needed to have enzyme activity..
I agree on Ray. I did research on partially purified enzyme before, on polyphenol oxidase, to be specific. I used only SEC to separate the enzyme from the protein pool (crude protein extract) and the results were frail. Nevertheless, it the specific enzyme activity increased as I continue to purify the enzyme.
Generally, if you continue to purify your protein, the protein concentration will decrease drastically. This will somewhat increase your specific enzyme activity, but reduces your overall yield.