Isolation of Trypsins by Affinity Chromatography

Neal C. Robinson; Ross W. Tye; Hans Neurath; Kenneth A. Walsh

doi:10.1021/bi00790a014

Isolation of Trypsins by Affinity Chromatography

Neal C. Robinson, Ross W. Tye, Hans Neurath, Kenneth A. Walsh

Department of Biochemistry & Structural Biology

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

2 Scopus citations

Abstract

Bovine α- and β-trypsin were separated by affinity chromatography on a column of chicken ovomucoid covalently bound to Sepharose. The two active fractions were selectively eluted by a pH gradient. The procedure was also applied to the purification of porcine and dogfish trypsins and to the isolation of trypsin from activated bovine pancreatic juice. Neither trypsinogen nor a-chymotrypsin was retarded by this column.

Original language	English (US)
Pages (from-to)	2743-2747
Number of pages	5
Journal	Biochemistry
Volume	10
Issue number	14
DOIs	https://doi.org/10.1021/bi00790a014
State	Published - Jul 1 1971

ASJC Scopus subject areas

Biochemistry

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title = "Isolation of Trypsins by Affinity Chromatography",

abstract = "Bovine α- and β-trypsin were separated by affinity chromatography on a column of chicken ovomucoid covalently bound to Sepharose. The two active fractions were selectively eluted by a pH gradient. The procedure was also applied to the purification of porcine and dogfish trypsins and to the isolation of trypsin from activated bovine pancreatic juice. Neither trypsinogen nor a-chymotrypsin was retarded by this column.",

author = "Robinson, {Neal C.} and Tye, {Ross W.} and Hans Neurath and Walsh, {Kenneth A.}",

year = "1971",

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AU - Tye, Ross W.

AU - Neurath, Hans

AU - Walsh, Kenneth A.

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Y1 - 1971/7/1

N2 - Bovine α- and β-trypsin were separated by affinity chromatography on a column of chicken ovomucoid covalently bound to Sepharose. The two active fractions were selectively eluted by a pH gradient. The procedure was also applied to the purification of porcine and dogfish trypsins and to the isolation of trypsin from activated bovine pancreatic juice. Neither trypsinogen nor a-chymotrypsin was retarded by this column.

AB - Bovine α- and β-trypsin were separated by affinity chromatography on a column of chicken ovomucoid covalently bound to Sepharose. The two active fractions were selectively eluted by a pH gradient. The procedure was also applied to the purification of porcine and dogfish trypsins and to the isolation of trypsin from activated bovine pancreatic juice. Neither trypsinogen nor a-chymotrypsin was retarded by this column.

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Isolation of Trypsins by Affinity Chromatography

Abstract

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