共 50 条
Modulation of protease activity to enhance the recovery of recombinant nucleocapsid protein of Nipah virus
被引:6
|作者:
Chong, Fui Chin
[1
,2
]
Tan, Wen Siang
[3
,4
]
Biak, Dayang Radiah Awang
[1
]
Ling, Tau Chuan
[4
,5
]
Tey, Beng Ti
[1
,4
]
机构:
[1] Univ Putra Malaysia, Dept Chem & Environm Engn, Fac Engn, Serdang 43400, Selangor, Malaysia
[2] Univ Malaysia Pahang, Dept Chem & Nat Resources Engn, Fac Engn, Kuantan 25000, Pahang, Malaysia
[3] Univ Putra Malaysia, Dept Microbiol, Fac Biotechnol & Biomol Sci, Serdang 43400, Selangor, Malaysia
[4] Univ Putra Malaysia, Inst Biosci, Serdang 43400, Selangor, Malaysia
[5] Univ Putra Malaysia, Dept Proc & Food Engn, Fac Engn, Serdang 43400, Selangor, Malaysia
关键词:
Endogenous protease;
Protease inhibitor;
Nucleocapsid protein;
Nipah virus;
Escherichia coli;
ESCHERICHIA-COLI;
CLEAVAGE;
INHIBITION;
CYSTEINE;
HENDRA;
SITE;
D O I:
10.1016/j.procbio.2009.08.012
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:
The nucleocapsid (N) protein of Nipah virus (NiV) expressed in Escherichia coli (E. coli) is antigenic and immunogenic. A method to enhance the recovery of recombinant N protein of NiV produced in E. coli is described. A bioinformatics tool, PeptideCutter was used to identify potential protease and cleavage sites from the amino acid sequences deduced from the published DNA sequence of the N protein of NiV. The size of degraded protein was estimated by using the Western blot and PeptideCutter analyse. The identified proteases were serine proteases, hence, a range of serine protease inhibitors were tested to improve the recovery of the N protein. The relative amount of N protein of NiV was 2-fold higher with the addition of PMSF, compared to the control sample (without any protease inhibitor supplementation). (C) 2009 Elsevier Ltd. All rights reserved.
引用
收藏
页码:133 / 137
页数:5
相关论文