Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell

C. S. Slater, T. G. Huggins, C. A. Brooks, H. C. Hollein

Research output: Contribution to journalArticlepeer-review

5 Scopus citations


The purification of a crude grade of bovine intestinal alkaline phosphatase by ultrafiltration has been studied. The purification process utilized a small stirred ultrafiltration cell operated in a batch mode to purify the enzyme. An Amicon YM100 membrane proved effective by recovering high amounts of enzyme activity and allowing the crude enzyme to be purged of its lower molecular weight impurities, which were mostly albumin. Studies were done utilizing various buffers, operating pressures, and stirrer speeds. Extensive investigation of the latter two parameters showed that stirrer speed was the most significant factor in decreasing flux decline and improving separation efficiency.

Original languageEnglish (US)
Pages (from-to)575-590
Number of pages16
JournalSeparation Science and Technology
Issue number6-7
StatePublished - Aug 1 1986
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Chemistry(all)
  • Chemical Engineering(all)
  • Process Chemistry and Technology
  • Filtration and Separation


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