卵白リゾチームの免疫化学的研究(第1報) : アセチル化したリゾチームについて

抄録

Hen egg white lysozyme was acetylated with acetic anhydride, the acetylated lysozyme was fractionated by carboxy methyl cellulose column chromatography, and three main peaks, termed F-I, F-II, and F-III, were obtained. The number of free amino groups in the acetylated lysozyme was determined by spectrophotometry using 2, 4, 6-trinitrobenzene-1-sulfonic acid. F-II and F-III possessed 4.6-4.8 unmodified amino groups per molecule and retained 7.5% of relative activity to Micrococcus lysodeikticus as compared to native lysozyme. Lysozyme moved faster than acetylated lysozyme to cathode in electrophoresis. In immunodiffusion, acetylated lysozyme (F-II and F-III) and lysozyme made a spur to antilysozyme serum. Quantitative precipitin reaction revealed that the antigenic determinants decreased by chemical modification. From these results, it may be concluded that acetylation of the amino groups alters the antigenic structure of lysozyme.