無および低カタラーゼ血症マウスのカタラーゼ分子の性質に関する研究

第1編 マウス肝カタラーゼ活性に対する変性剤の影響

抄録

Homogenates of mouse liver with isotonic sucrose solution were separated by the cell fractionation with repeating centrifugation. The supernatants were used for the inhibition test with the reagents such as 3, 5-diiodosalicylic acid lithium salt (LIS), guanidine and azide, heat, acid and alkali. After various treatments, the remaining catalase activities were measured and showed as a relative enzyme activity. Stability of catalase in liver supernatants was compared normal (C3H/C^a_sC^a_s) and mutant mice which were designated acatalasemia (C3H/C^b_sC^b_s), hypocatalasemia (C3H/C^c_sC^c_s) and acatalasemic heterozygote (C3H/C^a_sC^b_s).
In both treatments of LIS and guanidine, catalase of C^a_sC^a_s was most stable, C^b_sC^b_s were unstable, and catalase of C^c_sC^c_s and C^a_sC^b_s showed midle stability between the stability of C^a_sC^a_s and C^b_sC^b_s in this order. On the contrary in azide treatment within the range from O to 1 mM azide, C^b_sC^b_s was most stable, and C^a_sC^a_s, C^c_sC^c_s and C^a_sC^b_s were unstable in this order, but more than 1 mM azide, C^c_sC^c_s, C^a_sC^a_s and C^a_sC^b_s were unstable in this order. After incubation at various temperatures changing from 30°C to 60°C for 10 min, C^a_sC^a_s was most stable, and C^a_sC^b_s, C^c_sC^c_s and C^b_sC^b_s were unstable in this order. After acid and alkali treatments in the range of pH 5.5 to 9.0, relative activities of C^c_sC^c_s and C^a_sC^b_s were similar to that of C^a_sC^a_s, but C^b_sC^b_s was less stable than C^a_sC^a_s, C^c_sC^c_s and C^a_sC^b_s in the same range. It is considered that the structure of catalase molecule in the liver is different between normal, mutant mice and heterozigote of normal and mutant mice with regard to the difference of the stability to LIS, guanidine, azide, heat, acid and alkali treatments.