Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell

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

doi:10.1080/01496398608056136

Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell

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

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5 Scopus citations

Abstract

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 language	English (US)
Pages (from-to)	575-590
Number of pages	16
Journal	Separation Science and Technology
Volume	21
Issue number	6-7
DOIs	https://doi.org/10.1080/01496398608056136
State	Published - Aug 1 1986
Externally published	Yes

All Science Journal Classification (ASJC) codes

General Chemistry
General Chemical Engineering
Process Chemistry and Technology
Filtration and Separation

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10.1080/01496398608056136

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title = "Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell",

abstract = "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.",

author = "Slater, {C. S.} and Huggins, {T. G.} and Brooks, {C. A.} and Hollein, {H. C.}",

note = "Funding Information: Partial support for this work was provided by the National Science Foundation under Grant CPE 83-07486. Mr. John Nikityn is also acknowledged for his support of this work in addition to the Chemical Engineering Department of Manhattan College under the direction of Br. Conrad T. Burris, FSC.",

year = "1986",

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doi = "10.1080/01496398608056136",

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T1 - Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell

AU - Slater, C. S.

AU - Huggins, T. G.

AU - Brooks, C. A.

AU - Hollein, H. C.

N1 - Funding Information: Partial support for this work was provided by the National Science Foundation under Grant CPE 83-07486. Mr. John Nikityn is also acknowledged for his support of this work in addition to the Chemical Engineering Department of Manhattan College under the direction of Br. Conrad T. Burris, FSC.

PY - 1986/8/1

Y1 - 1986/8/1

N2 - 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.

AB - 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.

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Purification of Alkaline Phosphatase by Ultrafiltration in a Stirred Batch Cell

Abstract

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