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北京鸭LDH1提纯及其电泳分析

Purification and Electrophoretic Analysis of Heart LDH1 of Peking Duck

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【作者】 王素云宗健李美琴吴鹤龄

【Author】 Wang Suyun Zong Jian Li Meiqin Wu Heling (Department of Biology)

【机构】 北京大学生物系北京大学生物系

【摘要】 本文采用琼脂糖4B交联不溶性丙酮酸类似物(草酸盐衍生物)的亲和层析法及DEAE-Sephadex A50层析柱两种方法对北京鸭心肌LDH1进行分离纯化比较。 琼脂糖4B交联丙酮酸类似物层析柱具有高的亲和特性。比较经过亲和前后的样品通过DEAE-Sephadex A50柱二次纯化后,发现LDH同工酶在聚丙烯酰胺凝胶电泳图谱上出现二条具LDH酶活性的蛋白条带。其中LDH1的量远远超过LDH2的量。 在等电聚焦电泳的实验中,发现多肽现象电泳图谱表明LDH1有10条亚带。LDH2有9条亚带。

【Abstract】 We separated heart LDH, of Peking Duck by Sepharose-4B-CL-Oxamate affinity chromatography column and by DEAE-Sephadex A50 column.The Sepharose-4B-CL-Oxamate column has high affinity with LDH isoengyme. Eluant with an increasing solt gradient to 0.085M NaCl on DEAE-Sephadex A50 column. Two active bands of LDH isoengyme LDH1 and LDH2 were separated, while LDH1 was of more amount than that or LDH2. Protein pattern was obtained on PAGE plate. They are purified by Sepharose-4B-CL-Oxamate or by DEAE-Sephadex A50 column, or both. It was also found in the IEF test, that LDH1 Consested 10 subbands and. LDH2 of 9 subbands of polypeptiche pattern.

  • 【文献出处】 北京大学学报(自然科学版) ,Acta Scicentiarum Naturalum Universitis Pekinesis , 编辑部邮箱 ,1987年04期
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