Abstract:
:Culture conditions favouring the simultaneous formation of soluble protein and inclusion bodies (IBs) were chosen for producing the cytoplasmic protein beta-galactosidase or the periplasmic protein TEM-beta-lactamase. Soluble and insoluble cell fractions of Escherichia coli producing either beta-galactosidase or TEM-beta-lactamase were analyzed by one- and two-dimensional gel electrophoresis and subsequent silver staining or immunodetection of the recombinant protein. The results show that truncated fragments of the recombinant protein were not present in the soluble cell fraction but accumulate in the IB fraction. The presence of other cellular, non-plasmid-encoded proteins in IB preparations such as the outer membrane proteins OmpF, OmpC, and OmpA or the ribosomal subunit proteins L7/L12 was attributed to co-precipitation of cell-debris-associated components. Protein-folding enzymes were not detected in IB preparations. The specificity of in-vivo protein association in the formation of IBs and its implication on protein purification is discussed.
journal_name
Appl Microbiol Biotechnoljournal_title
Applied microbiology and biotechnologyauthors
Rinas U,Bailey JEdoi
10.1007/BF00240735subject
Has Abstractpub_date
1992-08-01 00:00:00pages
609-14issue
5eissn
0175-7598issn
1432-0614journal_volume
37pub_type
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