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 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.
Department of Pharmaceutical Sciences, University of Antwerp, Wilrijk, Belgium.
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Wang
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Hendriks
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Scharpé
D000327:Adsorption; D000596:Amino Acids / Q000737:chemistry*; D001920:Bradykinin / Q000031:analogs & derivatives / Q000737:chemistry; D002384:Catalysis; D003035:Cobalt / Q000737:chemistry; D003488:Cyanogen Bromide; D004800:Enzymes, Immobilized; D006801:Humans; D006868:Hydrolysis; D001121:Lysine Carboxypeptidase / Q000737:chemistry*; D010455:Peptides / Q000737:chemistry*; D012685:Sepharose; D015032:Zinc / Q000737:chemistry
D000596:Amino Acids; D004800:Enzymes, Immobilized; D010455:Peptides; C024626:bradykinin, des-Arg(9)-; D003035:Cobalt; D012685:Sepharose; D001121:Lysine Carboxypeptidase; D015032:Zinc; D003488:Cyanogen Bromide; D001920:Bradykinin