Isolation of carboxypeptidase N by affinity chromatography on column of CNBr-activated Sepharose with immobilized antibody
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Published:1979
Issue:2
Volume:44
Page:626-630
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ISSN:0010-0765
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Container-title:Collection of Czechoslovak Chemical Communications
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language:en
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Short-container-title:Collect. Czech. Chem. Commun.
Author:
Simonianová Eva,Petáková Marie
Abstract
The isolation of rat serum carboxypeptidase N (EC 3.4.2.2) by affinity chromatography on a column of CNBr-activated Sepharose with immobilized antibody is described. The ligands used were either rabbit antiserum to rat carboxypeptidase N or the IgG fraction prepared from this serum. The coupling of the isolated antibodies to CNBr-activated Sepharose increased the capacity of the column approximately three times. The specific activity of the enzyme prepared by this method was 109-times higher than the activity of the serum. Analysis of the final product by polyacrylamide gel electrophoresis showed carboxypeptidase N and traces of albumin.
Publisher
Institute of Organic Chemistry & Biochemistry
Subject
General Chemistry
Cited by
1 articles.
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