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The complete mature bovine prion protein highly expressed in Escherichia coli : biochemical and structural studies
Author(s) -
Negro Alessandro,
De Filippis Vincenzo,
Skaper Stephen D,
Sorgato M.Catia
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00798-9
Subject(s) - escherichia coli , gene isoform , histidine , prion protein , biochemistry , biology , escherichia , chemistry , microbiology and biotechnology , enzyme , gene , disease , medicine , pathology
According to the `protein only' hypothesis, modification of the 3‐dimensional fold of the constituent cellular protein, PrP C , into the disease‐associated isoform, PrP Sc , is the cause of neurodegenerative diseases in animals and humans. Here we describe the high‐level synthesis in Escherichia coli , and purification in the monomeric form, of a histidine‐tagged full‐length mature PrP (25–249) of bovine brain, termed His‐PrP. Based on biochemical and spectroscopic data, His‐PrP displays characteristics expected for the PrP C isoform. The reported expression system should allow the production of quantities of bovine PrP C sufficient to permit 3‐dimensional structure determinations.