Use of carboxypeptidase A for simultaneous assessment of purity and assignment of human Bence Jones proteins and light chains to K and L classes

A simple and rapid method involving the use of carboxypeptidase A was developed to assess the purity of human Bence Jones proteins and light chains and simultaneously to assign them to their principal antigenic class (K- or L-type). Only serine was released from purified L-type proteins by the actio...

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Bibliographic Details
Published inArchives of biochemistry and biophysics Vol. 132; no. 2; pp. 502 - 508
Main Authors Edmundson, Allen B., Simonds, Nanne B., Sheber, Florence A., Johnson, Timothy, Bangs, Betty
Format Journal Article
LanguageEnglish
Published United States Elsevier Inc 01.07.1969
Subjects
Amino Acids - analysis
Antigens - classification
Bence Jones Protein - classification
Carboxypeptidases
Chromatography, Gel
Humans
Immunoglobulin G - classification
Multiple Myeloma - immunology
Serine
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Summary:A simple and rapid method involving the use of carboxypeptidase A was developed to assess the purity of human Bence Jones proteins and light chains and simultaneously to assign them to their principal antigenic class (K- or L-type). Only serine was released from purified L-type proteins by the action of the enzyme, while no amino acids were liberated from K-type proteins. The heavy chain of a human myeloma IgG protein was also not susceptible to hydrolysis, but serine was released from the L-type light chain of the intact myeloma protein.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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ISSN:0003-9861
1096-0384
DOI:10.1016/0003-9861(69)90394-4