SPECIFICITY OF FACTOR-XA IN THE CLEAVAGE OF FUSION PROTEINS

被引:25
作者
HE, MG [1 ]
JIN, L [1 ]
AUSTEN, B [1 ]
机构
[1] ST GEORGE HOSP, SCH MED, DEPT SURG, PEPTIDE UNIT, LONDON SW17 0RE, ENGLAND
来源
JOURNAL OF PROTEIN CHEMISTRY | 1993年 / 12卷 / 01期
基金
英国惠康基金;
关键词
FACTOR-XA; FUSION PROTEINS; BACTERIAL EXPRESSION; PROTEOLYTIC SPECIFICITY;
D O I
10.1007/BF01024906
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 precursor protein honey bee prepromelittin has been expressed as a fusion protein in Escherichia coli joined to the C-terminus of a truncated form of the bacteriophage gene 10 protein via an engineered recognition sequence for Factor Xa. Factor Xa was found to cleave poorly at the engineered site, giving a low yield of the required prepromelittin. In contrast, cleavage on the C-terminal side of the sequence VLGR at residue 67 in the gene 10 sequence proceeded in high yield. Factor Xa may be inhibited by adjacent hydrophobic sequences on the C-terminal side of a potential cleavage site.
引用
收藏
页码:1 / 5
页数:5
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