title: Structural characterization of rabbit brain ubiquitin.
abstract: Ubiquitin has been isolated and purified from rabbit brain using gel permeation and reverse-phase high-performance liquid chromatography. The 76-residue protein exhibits one difference towards a murine form, is identical to other characterized vertebrate ubiquitins, and confirms an extensive conservation of the ubiquitin structure. No positional microheterogeneities were detectable between two sub-forms.
authors.affiliation: HEJ Research Institute of Chemistry, University of Karachi, Pakistan.
authors.forename: N
authors.initials: N
authors.lastname: Wajih
authors.forename: A R
authors.initials: AR
authors.lastname: Siddiqi
authors.forename: R
authors.initials: R
authors.lastname: Kaiser
authors.forename: B
authors.initials: B
authors.lastname: Persson
authors.forename: Z H
authors.initials: ZH
authors.lastname: Zaidi
authors.forename: H
authors.initials: H
authors.lastname: Jörnvall
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001923:Brain Chemistry; D017124:Conserved Sequence; D008969:Molecular Sequence Data; D011817:Rabbits; D017386:Sequence Homology, Amino Acid; D014452:Ubiquitins / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D014452:Ubiquitins