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Updated: Sep 17, 2026

Biochemical Titration of Glycogen In vitro
Published on: November 24, 2013
Glycogen-protein complexes as antigens
After immunization of rabbits with a glycogen-protein complex from muscles of spurge hawk-moth (Celerio euphorbiae Linnaeus 1758), the immunoglobulin fraction was isolated from the obtained antiserum. The antibody has been found to reach in the immunodiffusion and immunoelectrophoretic tests with glycogen from philogenetically remote species. After the reaction with the immunoglobulin fraction glycogen preparations were less effectively degraded by alpha-amylase. The results suggest that the protein component is responsible for antigenicity of the glycogen-protein complex. The antibody was used to localize the complex in the muscles by the indirect immunofluorescence test.
After immunization of rabbits with a glycogen-protein complex from muscles of spurge hawk-moth (Celerio euphorbiae Linnaeus 1758), the immunoglobulin fraction was isolated from the obtained antiserum. The antibody has been found to reach in the immunodiffusion and immunoelectrophoretic tests with glycogen from philogenetically remote species. After the reaction with the immunoglobulin fraction glycogen preparations were less effectively degraded by alpha-amylase. The results suggest that the protein component is responsible for antigenicity of the glycogen-protein complex. The antibody was used to localize the complex in the muscles by the indirect immunofluorescence test.
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