title: Purification and characterization of protein Z from rabbit liver cytosol.
abstract: Protein Z was purified from rabbit liver cytosol by affinity chromatography on oleic acid-agarose and preparative sodium dodecyl sulfate-polyacrylamide gel electrophoresis. After removal of sodium dodecyl sulfate, the renatured protein was found to bind heme and bilirubin with a Kd of approximately 1 microM which produced large red shifts in their absorption spectra. On isoelectric focusing, rabbit protein Z exhibited two main bands with pI around 6.0.
mesh_terms: D000818:Animals; D001663:Bilirubin / Q000378:metabolism; D002352:Carrier Proteins / Q000302:isolation & purification* / Q000378:metabolism; D003600:Cytosol / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D050556:Fatty Acid-Binding Proteins; D006418:Heme / Q000378:metabolism; D007525:Isoelectric Focusing; D008099:Liver / Q000032:analysis*; D011817:Rabbits; D051381:Rats; D013057:Spectrum Analysis
chemical_list: D002352:Carrier Proteins; D050556:Fatty Acid-Binding Proteins; D006418:Heme; D001663:Bilirubin