title: Purification and characterization of a basic 23 kDa cytosolic protein from bovine brain.
abstract: A soluble basic protein has been purified from bovine brain. It is constituted by a single polypeptide chain with a molecular weight of about 23 kDa and an isoelectric point of about 8.6. The protein was further characterized by its amino-acid composition and by a 39 amino-acid-long N-terminal sequence. Sequence homologies were demonstrated with some other cytosolic proteins. Ligand-binding assays revealed a significant affinity of the 23 kDa protein for bromosulfophthalein. Immunochemical analysis using a rabbit anti 23 kDa brain protein antiserum demonstrated its simultaneous presence in bovine liver as well as in soluble extracts from different origins (mouse and rat brain; human platelets).
mesh_terms: D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001923:Brain Chemistry; D002417:Cattle; D002846:Chromatography, Affinity; D003600:Cytosol / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D005779:Immunodiffusion; D007525:Isoelectric Focusing; D008099:Liver / Q000032:analysis; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000302:isolation & purification*; D013045:Species Specificity
chemical_list: D000596:Amino Acids; D009419:Nerve Tissue Proteins