Immobilized carboxypeptidase N : a potent bioreactor and specific adsorbent for peptides
Carboxypeptidase N-Sepharose was prepared by covalent immobilization of purified human plasma carboxypeptidase N. More than 98% of the carboxypeptidase N was immobilized; 42% of the applied activity can be detected on the support. The column has excellent capabilities to quantitatively remove carbox...
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Published in: | Applied biochemistry and biotechnology Vol. 44; no. 2; pp. 151 - 160 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
Heidelberg
Springer
01-02-1994
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Subjects: | |
Online Access: | Get full text |
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Summary: | Carboxypeptidase N-Sepharose was prepared by covalent immobilization of purified human plasma carboxypeptidase N. More than 98% of the carboxypeptidase N was immobilized; 42% of the applied activity can be detected on the support. The column has excellent capabilities to quantitatively remove carboxy-terminal basic amino acids from peptides, as is demonstrated using the synthetic peptide substrate hippuryl-L-arginine and the nonapeptide bradykinin, and remains stable for several months. In contrast with apocarboxypeptidase B-Sepharose, apocarboxypeptidase N-Sepharose poorly binds its substrates. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0273-2289 1559-0291 |
DOI: | 10.1007/BF02921652 |