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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Mechanism of salmon sperm decondensation by nucleoplasmin
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Mechanism of salmon sperm decondensation by nucleoplasmin

机译：核蛋白溶质解鲑精子的机理

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摘要

Removal of protamine from DNA-protamine (salmine, protamine from salmon sperm) complexes by nucleopasmin was examined and compared with that of poly-L-glutamic acid (PLGA) using turbidity and ethidium bromide (EB) treatment methods. When nucleoplasmin of PLGA was added to a DNA-protamine complex solution, turbidity was decreased and the amount of EB intercalated into DNA was increased. These results suggest that nucleoplasmin and PLGA can remove protamine from DNA-protamine complexes. The effect of nucleoplasmin was more potent than that of PLGA. Direct interaction of nucleoplasmin with protamine was confirmed by mixing experiments using circular dichrosim (CD) and fluorescence spectroscopies. Results suggest that uncleoplasmin is bound to protamine in a 1:1 ratio and that Trp~(126) is located near a hydrophilic region containing a polyglutamic acid tract of nucleoplasmin which was obviously influenced by its binding with protamine. It would appear that the polyglutamic acid tract in nucleoplasmin plays a critical role for binding with protamine.
机译：检查了核仁蛋白从DNA-鱼精蛋白（盐胺，鲑鱼精子中的鱼精蛋白）复合物中去除鱼精蛋白的方法，并使用浊度和溴化乙锭（EB）处理方法将其与聚L-谷氨酸（PLGA）的方法进行了比较。当将PLGA的核蛋白添加到DNA-鱼精蛋白复合物溶液中时，混浊度降低，而嵌入DNA的EB量增加。这些结果表明，核纤溶酶和PLGA可以从DNA-鱼精蛋白复合物中去除鱼精蛋白。核纤溶酶的作用比PLGA更有效。核纤溶蛋白与鱼精蛋白的直接相互作用通过使用圆二色胺（CD）和荧光光谱法进行的混合实验得以证实。结果表明，核纤溶酶与鱼精蛋白的结合比例为1：1，而Trp〜（126）位于含有核纤溶酶多谷氨酸束的亲水区域附近，显然受其与鱼精蛋白的结合的影响。看来核纤溶酶中的聚谷氨酸束对于与鱼精蛋白的结合起关键作用。

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