Molecular investigation on the interaction of spermine with proteinase K by multispectroscopic techniques and molecular simulation studies

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• 作者：Mansoore Hosseini-Koupaei^a ; Behzad Shareghi^a ; ^{b_shareghi@yahoo.com} ; Ali Akbar Saboury^b ; ^c ; Fateme Davar^d
• 关键词：Proteinase K ; Spermine ; Fluorescence spectroscopy ; Circular dichroism ; Catalytic activity ; Molecular simulation
• 刊名：International Journal of Biological Macromolecules
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：94
• 期：part_PA
• 页码：406-414
• 全文大小：1671 K
• 卷排序：94

文摘

Spermine could interact with proteinase K spontaneously at single binding site. The thermal stability of proteinase K increased upon spermine addition. Spermine can enhance the enzyme activity of proteinase K. Tertiary and secondary structural changes of proteinase K induced by spermine.