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SHORT COMMUNICATION

SHORT COMMUNICATION Introduction There is a strong clinical demand to quantitate urinary excretion of free immunoglubin ^ and -light-chains (Bence Jones proteins) by methods that can be mechanised, such as immunonephelometry or turbidimetry (1, 2). The "hidden" epitopes, specific for the free form of light-chains, are poor antigens. Moreover, di(oligo)merization of free light-chains in the urine obscures these epitopes (3). Alternatively, the use of antisera directed against bound ligth-chains, cross-reacting with the free form, has been advocated (4, 5). Usually, intact serum immunoglobulins are used for calibration of these assays. A number of theoretical considerations council against this approach: (i) The primary structure of the constant parts of free and bound lightrchains should be identical, but this does not necessarily apply to the secondary and tertiary structure. Differences in the epitopal architecture may result in differences in the antibody-antigen reaction with respect to the kinetics of precipitate formation and the size of the particles. This, in turn, Eur. J. Clin. Chem. Clin. Biochem. / Vol. 31,1993 / No. 6 dium dodecylsulfate gelelectrophoretic analysis and standard procedures (8). Ten ml aliquots were desalted by gel-filtration using a Sephadex G25 (Pharmacia, Freiburg) column (65 3.6 cm) equilibrated with 100 mmol/1 ammonium carbonate http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Clinical Chemistry and Laboratory Medicine de Gruyter

SHORT COMMUNICATION

Clinical Chemistry and Laboratory Medicine , Volume 31 (6) – Jan 1, 1993
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Publisher
de Gruyter
Copyright
Copyright © 2009 Walter de Gruyter
ISSN
1434-6621
eISSN
1437-4331
DOI
10.1515/cclm.1993.31.6.403
Publisher site
See Article on Publisher Site

Abstract

Introduction There is a strong clinical demand to quantitate urinary excretion of free immunoglubin ^ and -light-chains (Bence Jones proteins) by methods that can be mechanised, such as immunonephelometry or turbidimetry (1, 2). The "hidden" epitopes, specific for the free form of light-chains, are poor antigens. Moreover, di(oligo)merization of free light-chains in the urine obscures these epitopes (3). Alternatively, the use of antisera directed against bound ligth-chains, cross-reacting with the free form, has been advocated (4, 5). Usually, intact serum immunoglobulins are used for calibration of these assays. A number of theoretical considerations council against this approach: (i) The primary structure of the constant parts of free and bound lightrchains should be identical, but this does not necessarily apply to the secondary and tertiary structure. Differences in the epitopal architecture may result in differences in the antibody-antigen reaction with respect to the kinetics of precipitate formation and the size of the particles. This, in turn, Eur. J. Clin. Chem. Clin. Biochem. / Vol. 31,1993 / No. 6 dium dodecylsulfate gelelectrophoretic analysis and standard procedures (8). Ten ml aliquots were desalted by gel-filtration using a Sephadex G25 (Pharmacia, Freiburg) column (65 3.6 cm) equilibrated with 100 mmol/1 ammonium carbonate

Journal

Clinical Chemistry and Laboratory Medicine – de Gruyter

Published: Jan 1, 1993

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