Crystal Growth of Hen Egg-White Lysozyme (HEWL) under Various Gravity Conditions

被引:11
作者
Pan, Weichun [1 ]
Xu, Jin [2 ]
Tsukamoto, Katsuo [3 ]
Koizumi, Masako [3 ]
Yamazaki, Tomoya [3 ]
Zhou, Ru [1 ]
Li, Ang [1 ]
Fu, Yuying [1 ]
机构
[1] Zhejiang Gongshang Univ, Coll Food Sci & Biotechnol, Hangzhou 310035, Zhejiang, Peoples R China
[2] Wenzhou Univ, Coll Chem & Mat Engn, Wenzhou 325035, Zhejiang, Peoples R China
[3] Tohoku Univ, Sch Sci, Aoba Ku, Sendai, Miyagi 9808570, Japan
基金
中国国家自然科学基金;
关键词
Biocrystallization; Impurities; Microgravity Condition; lysozyme; PROTEIN CRYSTALS; NUCLEATION; MICROGRAVITY; ASSOCIATION; IMPURITIES; FERRITIN; KINETICS;
D O I
10.1016/j.jcrysgro.2013.04.056
中图分类号
O7 [晶体学];
学科分类号
0702 ; 070205 ; 0703 ; 080501 ;
摘要
Motivated by the enhancement of protein quality under microgravity condition, the behaviors of crystal growth under various gravity conditions have been monitored via Foton Satellite and parabolic flight. We found that the normal growth rate and the step velocity would be enhanced only at high protein concentration. Although the difference of diffusion between monomer lysozyme molecule and main impurity species in HWEL dimer may be able to explain this enhancement in long period at high protein concentration, it is not valid at low lysozyme concentration and it can't explain the results obtained by parabolic flight, in which microgravity condition maintained only about 20 s. In order to compromise this contradiction, cluster, universal existing in protein solution, has been picked up. The dynamic light scattering technique figured out dimer is served as the seed for cluster formation. Due to its large size, cluster keeps still under microgravity. Via this mechanism, the purification of lysozyme above crystal surface has been achieved. We also found the two supergravity (-1.5 g) periods immediately before and after microgravity period have different effects on the step velocity. The pre-MG period depresses the step velocity while the post-MG enhances it. This odd phenomenon ascribes to two factors: (1) the flow rate modification and (2) the purity of protein solution immediate above crystal surface. (C) 2013 Elsevier B.V. All rights reserved.
引用
收藏
页码:43 / 50
页数:8
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