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Detecting prion protein gene mutations by denaturing gradient gel electrophoresis
Author(s) -
Fink John K.,
Peacock Michael L.,
Warren James T.,
Roses Allen D.,
Prusiner Stanley B.
Publication year - 1994
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.1380040106
Subject(s) - biology , temperature gradient gel electrophoresis , fatal familial insomnia , gene , coding region , genetics , haplotype , prion protein , point mutation , gene sequence , sequence (biology) , mutation , microbiology and biotechnology , disease , allele , pathology , medicine , 16s ribosomal rna , phylogenetic tree
Mutations of the prion protein (PrP) gene are present in patients with Gerstmann–Sträussler–Scheinker syndrome (GSS), familial Creutzfeldt–Jakob disease (CJD), and fatal familial insomnia (FF1). We developed a denaturing gradient gel electrophoresis (DGGE) strategy that readily identifies point mutations in the PrP coding sequence. By comparison with appropriate controls, haplotypes often may be deduced. This method permits samples from many patients with GSS, CJD, as well as patients with unusual degenerative neurologic disorders, to be screened rapidly, sensitively, and inexpensively for the presence of known and novel PrP mutations. We illustrate the sensitivity of this approach by reporting 2 novel polymorphisms in the PrP coding sequence. © 1994 Wiley‐Liss, Inc.