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what results match the characteristics of AP in a native gel and a sds gel- electrophoresis?

what results match the characteristics of AP in a native gel and a sds gel- electrophoresis?

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In native gel electrophoresis the protein ( that is not denaturated) migrates according to its charge, (hydrodynamic) size and shape.

By denaturation with SDS, the protein loose its three-dimensional structure. The protein is separated in sub-units, separated according only to their molecular mass. The charge density of sub-units is uniform, i.e., the same negative charge per mass unit. By using markers for molecular mass, sub-units (fractions/monomers) can be characterized for their mass.

The AP (Alkaline Phosphatase) isoenzymes are usually separated by electrophoresis. The electrophoretic mobilities in native forms are quite similar.

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