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Purification of swine kidney alkaline phosphatase by immunoaffinity chromatography

✍ Scribed by Shinichiro Oida; Masae Sone; Satoshi Sasaki

Publisher
Elsevier Science
Year
1984
Tongue
English
Weight
280 KB
Volume
140
Category
Article
ISSN
0003-2697

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✦ Synopsis

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.

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