title: Full-size form of human liver AMP-deaminase?
abstract: AMP-deaminase from human liver was purified by two-step phosphocellulose chromatography, and SDS-PAG electrophoresis of the most active enzyme fraction eluted has been performed. The largest of the protein fragments revealed had a size (92 kDa) of an apparent full-size enzyme subunit, and reacted positively with antibodies produced against specific human ampd2 gene product. Three-day storage at cold room temperature modified significantly the electrophoretical pattern of the enzyme, evidencing continuous and progressive degradation of its structure. This is a first report evidencing the presence of apparent full-size form of human liver AMP-deaminase in preparation obtained from endogenous source.
authors.affiliation: Department of Biochemistry, Medical University of Gdansk, Debinki, Gdansk, Poland. mgazda@amg.gda.pl
authors.forename: M
authors.initials: M
authors.lastname: Szydlowska
authors.forename: Z
authors.initials: Z
authors.lastname: Chodorowski
authors.forename: I
authors.initials: I
authors.lastname: Rybakowska
authors.forename: G
authors.initials: G
authors.lastname: Nagel-Starczynowska
authors.forename: K
authors.initials: K
authors.lastname: Kaletha
mesh_terms: D000659:AMP Deaminase / Q000737:chemistry* / Q000302:isolation & purification*; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000302:isolation & purification; D008099:Liver / Q000201:enzymology*; D008970:Molecular Weight
chemical_list: D007527:Isoenzymes; D000659:AMP Deaminase