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Purification and partial amino acid sequencing of bovine kidney alkaline phosphatase
The International Journal of Biochemistry
|January 1, 1987
Abstract:
Bovine kidney alkaline phosphatase (ALPase) was purified by the sequential application of monoclonal anti-bovine cartilage ALPase affinity, DEAE-cellulose, and Sepharose CL-6B chromatography. Sodium dodecyl sulfate-polyacrylamide-gel electrophoresis showed the presence of a single band corresponding to a molecular weight of 80,000. The N-terminal amino acid sequence of bovine kidney alkaline phosphatase was determined as follows: Leu-Val-Pro-Glu-Lys-Asp-Pro-?-Tyr-Trp-Arg-Asp-Gln-Ala-Gln.