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Purification of swine kidney alkaline phosphatase by immunoaffinity chromatography
Analytical Biochemistry
|July 1, 1984
Abstract:
A homogeneous alkaline phosphatase preparation was obtained from swine kidney cortex by a simple purification step of immunoaffinity chromatography. The enzyme was purified 426 times that of the initial acetone powder with a recovery of 69.6% and a specific activity of 1206 units/mg of protein. The sodium dodecyl sulfate-gel electrophoretic pattern showed a single 80,000-Mr protein band as the monomer of the purified enzyme.