Studies on Biotransformation of Lysozyme. IV. Radioimmunoassay of Lysozyme and Its Evaluation

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The radioimmunoassay of hen egg-white lysozyme (hen lysozyme) was investigated and evaluated in order to examine the biotransformation of the enzyme in men. ^<125>I-labeled hen lysozyme was prepared and separation of the free from the bound form of the enzyme was performed by dextran-treated charcoal method in comparison with two-antibody method. From the result, it was idnicated that dextran-treated charcoal method was useful from the viewpoint of precision, reproducibility and simplicity. The stability of hen lysozyme labeled was determined by the degree of radioactivity bound to antibody. The recovery of radioactivity bound to antibody decreased with the time lapse after labeling and it was found that the recovery rate was restored by dialysis. In this radioimmunoassay system, the competitive binding of labeled and unlabeled hen lysozyme to antibody was examined, and 0.3 to 5.0ng/ml of the enzyme were detectable. It was found that human lysozyme had an influence on the radioimmunoassay system with over 2μg/ml. But, the influence did not disturb the assay of hen lysozyme in human serum. Additionally, since it was found that the ratio of the bound form to the free increased with human serum, the assay of hen lysozyme in human serum was carried out using a calibration curve of the enzyme added to untreated human serum. Thus, human serum levels after oral administration of hen lysozyme were measured by the radioimmunoassay in comparison with the determination method by lytic activity. This radioimmunoassay system was found to be appropriate for the determination of hen lysozyme in human serum.
公益社団法人日本薬学会の論文
1978-03-25

Studies on Biotransformation of Lysozyme. IV. Radioimmunoassay of Lysozyme and Its Evaluation

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