[Electrophoresis of serum lipoproteins in man and normal adult dogs. Remarks on experiments].
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Biomedical subjects
Publications and source records attributed to J Groulade.
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Thirty human cryoglobulin precipitates obtained from 21 patients were fixed and examined by electron microscopy; following biochemical isolation and identification. This study showed that the fine structure of cryoprecipitates depends on the involved immunoglobulins and on their respective quantities. Monoclonal IgG kappa 1 or 3 cryoglobulins with antibody activity form crystalling precipitates of 22-nm diameter rods and annuli. When polyclonal, they form 6-nm-wide filaments. Mixed IgG and IgM cryoprecipitates appear as cylindric and annular bodies with an internal diameter of 12 nm and a total diameter of 62 nm. When IgM predominates over IgG, globular condensations with a diameter of 30 nm are seen. Mixtures in which the IgG is more abundant than the IgM include fingerprint-like periodic condensations.
A technique is described which combines ultracentrifugation in a density gradient stabilized by gelification, with agar gel immunodiffusion. The use of this procedure to determine sedimentation parameters and antigenic determinations is presented and illustrated with the diagramms obtained in the identification of various cryoglobulins.
The determination of the location of serum proteins after electrophoresis on various supports and after immunoelectrophoresis has been achieved by immunochemical methods with specific antisera. The present study describes the technique, gives details of various identified fractions and presents some figures. The method allows us to study the constitution of the "beta-gamma block" observed on paper and acetate supports after electrophoresis of cirrhotic sera and to superimpose the patterns of apparently distinct fractions on polyacrylamide gel.
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