Purification of acid-proteases by affinity partitioning in aqueous two-phase systems

Jyh Ping Chen; Alfred Carlson

doi:10.1007/BF00155466

Purification of acid-proteases by affinity partitioning in aqueous two-phase systems

Jyh Ping Chen^*, Alfred Carlson

^*Corresponding author for this work

Pennsylvania State University

Research output: Contribution to journal › Journal Article › peer-review

4 Scopus citations

Abstract

An affinity polymer derivative was synthesized with the group specific acid protease inhibitor pepstatin attached to dextran (M.W. 500,0001). This derivative was used in an aqueous two-phase system with hydroxypropyldextran to purify crude solutions of chymosin and Endothia parasitica (EP) acid proteases. Chymosin was purified by a factor of 6.2 with an overall yield of 83%. EP protease was similarly purified. A new pepstatin binding protease was discovered in crude EP extracts.

Original language	English
Pages (from-to)	263-268
Number of pages	6
Journal	Biotechnology Techniques
Volume	1
Issue number	4
DOIs	https://doi.org/10.1007/BF00155466
State	Published - 12 1987
Externally published	Yes

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title = "Purification of acid-proteases by affinity partitioning in aqueous two-phase systems",

abstract = "An affinity polymer derivative was synthesized with the group specific acid protease inhibitor pepstatin attached to dextran (M.W. 500,0001). This derivative was used in an aqueous two-phase system with hydroxypropyldextran to purify crude solutions of chymosin and Endothia parasitica (EP) acid proteases. Chymosin was purified by a factor of 6.2 with an overall yield of 83\%. EP protease was similarly purified. A new pepstatin binding protease was discovered in crude EP extracts.",

author = "Chen, \{Jyh Ping\} and Alfred Carlson",

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AU - Carlson, Alfred

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N2 - An affinity polymer derivative was synthesized with the group specific acid protease inhibitor pepstatin attached to dextran (M.W. 500,0001). This derivative was used in an aqueous two-phase system with hydroxypropyldextran to purify crude solutions of chymosin and Endothia parasitica (EP) acid proteases. Chymosin was purified by a factor of 6.2 with an overall yield of 83%. EP protease was similarly purified. A new pepstatin binding protease was discovered in crude EP extracts.

AB - An affinity polymer derivative was synthesized with the group specific acid protease inhibitor pepstatin attached to dextran (M.W. 500,0001). This derivative was used in an aqueous two-phase system with hydroxypropyldextran to purify crude solutions of chymosin and Endothia parasitica (EP) acid proteases. Chymosin was purified by a factor of 6.2 with an overall yield of 83%. EP protease was similarly purified. A new pepstatin binding protease was discovered in crude EP extracts.

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DO - 10.1007/BF00155466

M3 - 文章

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VL - 1

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JO - Biotechnology Techniques

JF - Biotechnology Techniques

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ER -

Purification of acid-proteases by affinity partitioning in aqueous two-phase systems

Abstract

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