水晶體 α-Crystallin의 Methylation = Methylation of α-Crystallin of bovine lens

다국어 초록 (Multilingual Abstract)

The elution profile of nonmethylated and endogenous methylated soluble fraction protein of bovine lens are compared by sephacryl S-300 chromatography, and then changes of protein patterns of nonmethylated and methylated α-crystallin fractions have been investigated by urea/ polyacrylamide gel electrophoresis.
1. The nonmethylated and methylated soluble fraction proteins are analyzed by sephacryl S-300 chromatography. In the nonmethylated protein four peaks are eluted in the tube NO. 21, 30, 34, 38 and identified as α, β_H,β_L,γ-crystallin, but eluted in the tube NO. 20, 29, 32, 36 in methylated protein, respectively.
2. When the soluble fraction of lens is methylated with S-adenosyl-L- [methyl-³H] methionine and separated by sephacryl S-300 chromatography, 90% of radioactivity is detected in α-crystallin fraction.
3. Nonmethylated α-crystallin is separated eight subfractions by urea/polyacrylamide gel electrophoresis. In the methylated α-crystallin, subfraction NO. 6,7 are disappeared and NO. 4, 5 are increased when compared with that of nonmethylated.
From the above result, it is suggested that endogenous methylation of α-crystallin of lens by protein methylase Ⅱ may be related to the formation of high molecular weight protein.

목차 (Table of Contents)

• 목차
• I. 緖論 = 1
• II. 實驗材料 및 方法 = 1
• III. 實驗成績 = 2
• IV. 考察 = 4
• V. 結論 = 4
• 參考文獻 = 5
• Summary = 6