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...

Full description

Saved in:
Bibliographic Details
Published in:Applied biochemistry and biotechnology Vol. 44; no. 2; pp. 151 - 160
Main Authors: WEI WANG, HENDRIKS, D. F, SCHARPE, S. L
Format: Journal Article
Language:English
Published: Heidelberg Springer 01-02-1994
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02921652