Intense Pulsed Electric Fields Denature Urease Protein

被引:9
作者
Urabe, Gen [1 ]
Katagiri, Toshiaki [1 ]
Katsuki, Sunao [2 ]
机构
[1] Kumamoto Univ, Grad Sch Sci & Technol, Kumamoto, Japan
[2] Kumamoto Univ, Inst Pulsed Power Sci, Kumamoto, Japan
来源
BIOELECTRICITY | 2020年 / 2卷 / 01期
关键词
nanosecond pulsed electric field (nsPEF); protein; slight thermal effect; intracellular condition; ALUMINUM; OVEREXPRESSION; OPTIMIZATION; PURIFICATION; AGGREGATION;
D O I
10.1089/bioe.2019.0021
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Background: This article describes the effects of nanosecond pulsed electric fields (nsPEFs) on the structure and enzyme activity of three types of proteins. Materials and Methods: Intense (up to 300kV/cm) 5-ns-long electrical pulses were applied for 500 times at 3Hz to solutions of lysozyme, albumin, and urease. We analyzed covalent bonds (peptide bonds and disulfide bonds) of lysozyme and albumin, and also the tertiary and quaternary structures of urease as well as urease activity. Results: The results indicated deformation of both the quaternary and tertiary structures of urease upon exposure to an electric field with an amplitude of 250kV/cm or higher, whereas no structural changes were observed in lysozyme or albumin, even at 300kV/cm. The enzyme activity of urease also decreased at field strengths of 250kV/cm or higher. Conclusion: Our experiments demonstrated that intense nsPEFs physically affected the conformation and function of some types of proteins. Such intense electric fields often occur in cell membranes when exposed to a moderate pulsed electric field.
引用
收藏
页码:33 / 39
页数:7
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