THE COMPLETE MATURE BOVINE PRION PROTEIN HIGHLY EXPRESSED IN ESCHERICHIA-COLI - BIOCHEMICAL AND STRUCTURAL STUDIES

Citation
A. Negro et al., THE COMPLETE MATURE BOVINE PRION PROTEIN HIGHLY EXPRESSED IN ESCHERICHIA-COLI - BIOCHEMICAL AND STRUCTURAL STUDIES, FEBS letters, 412(2), 1997, pp. 359-364
Citations number
36
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
412
Issue
2
Year of publication
1997
Pages
359 - 364
Database
ISI
SICI code
0014-5793(1997)412:2<359:TCMBPP>2.0.ZU;2-8
Abstract
According to the 'protein only' hypothesis, modification of the 3-dime nsional fold of the constituent cellular protein, PrPC, into the disea se-associated isoform, PrPSc, is the cause of neurodegenerative diseas es in animals and humans, Here we describe the high-level synthesis in Escherichia coli, and purification in the monomeric form, of a histid ine-tagged full-length mature PrP (25-249) of bovine brain, termed His -PrP, Based on biochemical and spectroscopic data, His-PrP displays ch aracteristics expected for the PrPC isoform, The reported expression s ystem should allow the production of quantities of bovine PrPC suffici ent to permit 3-dimensional structure determinations. (C) 1997 Federat ion of European Biochemical Societies.