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Expression and stability of the hepatitis B pol protein in Escherichia coli
Author(s) -
LIN CG.,
YOU LR.,
LO S. J.
Publication year - 1993
Publication title -
journal of gastroenterology and hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.214
H-Index - 130
eISSN - 1440-1746
pISSN - 0815-9319
DOI - 10.1111/j.1440-1746.1993.tb01683.x
Subject(s) - fusion protein , escherichia coli , microbiology and biotechnology , western blot , biology , glutathione s transferase , gene , glutathione , biochemistry , enzyme , recombinant dna
The pGEX plasmid containing the gene of glutathione S‐transferase (GST) was employed to express various lengths of the hepatitis B virus pol protein in a form of fusion protein in Escherichia coli. Results of SDS‐PAGE and Western blot analyses indicated that: (i) expression of GST‐pol fusion proteins varied from undetectable to 30% of total protein in different clones; (ii) presence of the carboxyl terminus of the pol protein apparently lowered the expression amount of fusion proteins; (iii) some distinct pol protein bands of lower molecular weight were constantly detected in several clones. The presence of the smaller pol protein therefore raises a possibility that the pol protein contains protease cutting sites.