The Isolation of Chymotrypsin-Like Enzymes by Affinity Chromatography Using Sepharose–4-Phenyibutyiamine
Affinity chromatography of chymotrypsin-like proteases on a column of Sepharose–4-phenylbutylamine (PBA) has been developed. Sepharose–PBA (Sepharose–NH∙[CH 2 ]4∙C 6 H 5 ) has been shown to selectively adsorb chymotrypsin α and B from weakly alkaline solutions and to allow to pass through unretarded...
Published in: | Canadian Journal of Biochemistry |
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Main Authors: | , |
Format: | Article in Journal/Newspaper |
Language: | English |
Published: |
Canadian Science Publishing
1971
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Subjects: | |
Online Access: | http://dx.doi.org/10.1139/o71-017 http://www.nrcresearchpress.com/doi/pdf/10.1139/o71-017 |
Summary: | Affinity chromatography of chymotrypsin-like proteases on a column of Sepharose–4-phenylbutylamine (PBA) has been developed. Sepharose–PBA (Sepharose–NH∙[CH 2 ]4∙C 6 H 5 ) has been shown to selectively adsorb chymotrypsin α and B from weakly alkaline solutions and to allow to pass through unretarded porcine trypsin, bovine trypsinogen, and chymotrypsin α modified with active-site-directed irreversible inhibitors. Chymotrypsinogen A and bovine trypsin were only slightly retarded whereas a preparation of subtilisin was markedly retarded and separated into two distinct peaks. Sepharose–PBA has been utilized successfully for the selective isolation of chymotryps in-like proteases from extracts of moose pancreas (Alces alces). |
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