Immunoglobulin heterogeneity in the rainbow trout, Salmo gairdneri Richardson

Abstract. Hetereogeneity of rainbow trout immunoglobulins was demonstrated by using monoclonal antibody 1A6 and polyacrylamide‐gradient gel electrophoresis. Immunoglobulins defined by elisa using monoclonal antibody 1A6 were about 30% of the total immunoglobulins, detected by elisa using polyclonal antibodies, in healthy rainbow trout. In trout obtained from farms with a previous history of infectious viral diseases, 1A6‐immunoglobulins were only about 14% of the total. Several serum pools from infected trout could be totally depleted of 1A6‐immunoglobulins (about 12% of total immunoglobulins) by affinity chromatography over Sepharose immobilized monoclonal antibody 1A6. Polyacrylamide‐gradient gel electrophoresis under denaturing conditions of total immunoglobulins, 1A6 immunoglobulins and no‐1A6 immunoglobulins purified by affinity chromatography, showed a majority heavy chain of 70 KDa and a minority heavy chain of about 60 KDa, two light chains of 24 and 26 KDa, and a 11–14 KDa polypeptide. Copyright © 1989, Wiley Blackwell. All rights reserved

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Bibliographic Details
Main Authors: Sanchez, C., Dominguez, J., Coll, J.
Format: journal article biblioteca
Language:eng
Published: 1989
Online Access:http://hdl.handle.net/20.500.12792/5457
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Summary:Abstract. Hetereogeneity of rainbow trout immunoglobulins was demonstrated by using monoclonal antibody 1A6 and polyacrylamide‐gradient gel electrophoresis. Immunoglobulins defined by elisa using monoclonal antibody 1A6 were about 30% of the total immunoglobulins, detected by elisa using polyclonal antibodies, in healthy rainbow trout. In trout obtained from farms with a previous history of infectious viral diseases, 1A6‐immunoglobulins were only about 14% of the total. Several serum pools from infected trout could be totally depleted of 1A6‐immunoglobulins (about 12% of total immunoglobulins) by affinity chromatography over Sepharose immobilized monoclonal antibody 1A6. Polyacrylamide‐gradient gel electrophoresis under denaturing conditions of total immunoglobulins, 1A6 immunoglobulins and no‐1A6 immunoglobulins purified by affinity chromatography, showed a majority heavy chain of 70 KDa and a minority heavy chain of about 60 KDa, two light chains of 24 and 26 KDa, and a 11–14 KDa polypeptide. Copyright © 1989, Wiley Blackwell. All rights reserved