title: Preparation and crystallization of human transthyretin (prealbumin) variants.
abstract: Naturally occurring variants of human serum transthyretin (prealbumin) have been prepared by recombinant DNA methods and crystallized from ammonium sulfate solutions to give crystals suitable for x-ray crystallographic analysis. Included are variants which are known to be associated with familial amyloidotic polyneuropathy. Dyes which have been used as histochemical stains to identify amyloid tissue deposits: Congo Red, Methylene Blue and Bromophenol Blue, have been co-crystallized with the transthyretin variants. Congo Red was found to be very selective while Methylene Blue actually assisted in the formation of crystals. All crystal forms which were examined were isomorphous to the structure of normal transthyretin.
authors.affiliation: Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis 46202-5122.
authors.forename: L K
authors.initials: LK
authors.lastname: Steinrauf
authors.forename: Y J
authors.initials: YJ
authors.lastname: Cao
authors.forename: J
authors.initials: J
authors.lastname: Hamilton
authors.forename: J
authors.initials: J
authors.lastname: Murrell
authors.forename: J J
authors.initials: JJ
authors.lastname: Liepnieks
authors.forename: M D
authors.initials: MD
authors.lastname: Benson
mesh_terms: D001483:Base Sequence; D003460:Crystallization; D003461:Crystallography; D004926:Escherichia coli; D006801:Humans; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D011228:Prealbumin / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins
chemical_list: D011228:Prealbumin; D011994:Recombinant Proteins