NR AIVC
AU Negro,A.; de Filippis,V.; Skaper,S.D.; James,P.; Sorgato,M.C.
TI The complete mature bovine prion protein highly expressed in Escherichia coli: biochemical and structural studies.
QU FEBS Letters 1997 Jul 28; 412(2): 359-64
PT journal article
AB According to the 'protein only' hypothesis, modification of the 3-dimensional fold of the constituent cellular protein, PrPc, into the disease-associated isoform, PrPsc, 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 PrPc isoform. The reported expression system should allow the production of quantities of bovine PrPc sufficient to permit 3-dimensional structure determinations.
IN Die Autoren berichten, dass sie in E.coli große Mengen des normalen Rinder-Prionproteins exprimieren können.
ZR 36
MH Amino Acid Sequence; Animal; Cattle; Chromatography, Affinity; Circular Dichroism; Cloning, Molecular; Electrophoresis, Polyacrylamide Gel; Endopeptidase K/metabolism; Escherichia coli/genetics; Molecular Sequence Data; Prions/*genetics/isolation & purification/metabolism; Protein Conformation; Spectrophotometry, Ultraviolet; Support, Non-U.S. Gov't
AD Dipartimento di Chimica Biologica, Centro CNR dello Studio delle Biomembrane, Universita di Padova, Padua, Italy.
SP englisch
PO Niederlande
OR Prion-Krankheiten 6