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缢蛏两种碱性磷酸酯酶与十二烷基磺酸锂作用过程中构象与活力变化的差异

Changes in Conformation and Catalytic Activity of Two Forms of Alkaline Phosphatase-from Sinonovacula Constricta During Denaturation by Lithium Dodecyl Sulfate

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【作者】 颜思旭; 余卫平;

【Author】 Yan Sixu Yu Weiping (Biology Department)

【机构】 厦门大学生物学系; 厦门大学生物学系;

【摘要】 <正> 碱性磷酸酯酶(Alkaline phosphatase E.C.3,1.3.1.简称AKP)广泛存在于微生物界与动物界,它是催化水解磷酸单酯键,对物质代谢具有重要作用的水解酶。对它的研究已有很多报导。但对于软体动物中AKP的研究,国外报导极少,国内尚属空白。我可根据自己的工作从缢蛏软体动物门,瓣鳃纲,竹蛏科,(Sinonovacula constricata)中

【Abstract】 Two different alkaline phosphatase forms (AKP Ⅰ & AKP Ⅱ)were isolated and purified from Sinonovacula constricta.Their molecular weights were 420,030 and 133,000 dultons respectively.The two purified enzymes were all found to be homogeneous by polyacrylaraide gel electrophoresir.The effect of LDS on AKP Ⅰ & AKP Ⅱ have been investigated by means of fluorescence and UV difference spectra.The three-dimensional structures of AKP Ⅰ &AKP Ⅱ are different and reveal a great diversity on behaviour,At high concentrations of LDS,both ARP Ⅰ & AKPⅡ maintained high residual activities.

  • 【文献出处】 厦门大学学报(自然科学版) ,Journal of Xiamen University(Natural Science) , 编辑部邮箱 ,1985年01期
  • 【被引频次】10
  • 【下载频次】47
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