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水晶體 α-Crystallin의 Aggregation에 對한 Calcium의 影響에 關한 硏究
郭明憲,林圭,郭相太,黃炳斗 충남대학교 의과대학 지역사회의학연구소 1987 충남의대잡지 Vol.14 No.2
The elution profile of CaCI_2 treated and EGTA plus CaC1_2-treated soluble fraction protein of bovine lens are compared by Sephacryl S-300 chromatography, and then changes of protein patterns of CaCI_2-treated crystallin and EGTA plus CaCI_2-treated α-crvstallin fractions have been investigated by urea/polyacrylamide gel electrophoresis. 1. In the presence of 0.8 mM CaCI_2, 10 mM CaCI_2, or 10 mM CaCI_2 plus 20 MM EGTA, absorbance at 500 nm exhibited 0.039, 0.087, 0.040 respectively. 2. Physiologic concentration (0.8 mM) CaCI_2-treated, 10 mM CaCI_2-treated and 10 mm CaCI_2 plus 20 mM EGTA-treated soluble fractions were analyzed by Sephacryl S-300 chromatography. In the 0. 8 mM CaCI_2-treated proteins four peaks were eluted in the tube No. 17, 27, 31, 35 and identified as α, β_H, β_L, γ-crystallin, but eluted in the tube No. 16, 26, 30, 33 in 10 mM CaCI_2-treated protein, respectively. In presence of 10 mM CaCI_2 plus 10 mM EGTA, protein patterns exhibited the same. 3. Physiological concentration (0. 8 mM) CaC_2-treated α-crystallin was seperated ten subtractions by urea/polyacrylamide gel electrophoresis. In the 10 mM CaCI_2-treated α-crystallin, No. 9 subfraction was disappeared and No. 3B was newly appeared when compared with that of 0.8 mM CaCI_2 treated and 10 mM CaCI_2 plus 20 mM EGTA. 4. Absorbance and electrophoretic pattern of 10mM CaCI_2-treated native a-crystallin exhibited the same result of 0.8 mM CaCI_2-treated. 5. Ten inilimoles mercaptoethanol treated soluble fraction protein exhibited the same elution profile when compared with nontreated soluble fraction proteins. From the above results, it is suggested that the aggregation of a-crystallin of lens by calcium may be resulted to the interaction of (β,γ-crystallin, and not related the formation of disulfide bond.