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Fusion expression of human pro‐urokinase with E. coli thioredoxin
Author(s) -
Sun AiLong,
Hua ZiChu,
Yao Ju,
Yang YongHua,
Yin DaQiang
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800204002
Subject(s) - inclusion bodies , thioredoxin , escherichia coli , fusion protein , protein disulfide isomerase , plasmid , biochemistry , recombinant dna , chemistry , microbiology and biotechnology , biology , disulfide bond , enzyme , gene
Human pro‐urokinase (pro‐UK) was cloned into plasmid pET32b and fused to the E. coli thioredoxin (trxA). When expressed in E. coli AD494(DE3), the fusion protein Trx‐pro‐UK accumulated as insoluble inclusion bodies and amounted to 35% of total cellular proteins. When co‐expressed with molecular chaperones human protein disulfide isomerase (PDI) and E. coli GroESL, all the expressed products still existed in the form of insoluble inclusion bodies.