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水晶體의 Protein Methylase Ⅱ에 關한 硏究
金炳鎬,김익수 충남대학교 의과대학 지역사회의학연구소 1984 충남의대잡지 Vol.11 No.1
Protein methylase II has been purified from bovine lens approximately 2,290-fold with a 5% yield. The enzyme shows a sharp pH optimum around pH 5.8. The enzyme is easily inactivated by heat treatment for 5 minutes at 70℃, and when stored at -20℃, even in the presence of 10% glycerol and 1 mM dithiothreitol, approximately 70℃ activity has been lost in a day. Cu^2+ is a potent inhibitor, 70% of activity being inhibited at 2 mM, and the enzyme activity with α-crystallin as substrate was increased about-40% in the presence of 2 mM Fey^2+. α-Crystallin, β_H-crystallin and histone IIA were found to be good substrates for this enzyme with preference for α-crystallin. The Km value for S-adenosyl-methionine is 1. 16 x 10^-6 M. Protein methylase II is the most abundant in the lens among the eye tissues. The specific activity of protein methylase II is higher in the nuclear portion(5. 8 pmoles/mg/min) than in the cortical portion (4.7 pmoles/mg/min). When the 39, 000xg-supernatant fraction of lens is methylated with S-adenosyl-L-〔methyl-^3H〕 methionine, 90% of radioactivity is detected in α-crystallin fraction by sephacryl S-300 chromatography. The effect of protein methylation on the aggregation of lens protein is examined by mixing methylated α-crystallin with ^14C-methylated, β_H-crystallin or with ^14C-methyaated γ-crystallin. The mixture is chromatographed on sephacryl S-300 and it is found that 53% and 33% radioactivity are detected in α-crystallin fraction, respectively. From the above results, it is suggested that protein methylase II may be involved in cataracgenesis and aging process in the lens.
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