A Chicken Transferrin Binding Protein Is Heat Shock Protein 108

• Published in: Biochemical and biophysical research communications Vol. 200; no. 1; pp. 65 - 70
• Main Authors: Hayes, G.R., Himpler, B.S., Weiner, K.X.B., Lucas, J.J.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.04.1994
• Subjects: Amino Acid Sequence; Animals; Antibodies, Monoclonal; Blotting, Western; Carrier Proteins - chemistry; Carrier Proteins - isolation & purification; Cell Membrane - metabolism; Chickens; Chromatography, Affinity; Chromatography, High Pressure Liquid; Electrophoresis, Polyacrylamide Gel; ESTRES TERMICO; FEMELLE; GLOBULINAS; GLOBULINE; HEMBRA; Iron-Binding Proteins; Liver - metabolism; Molecular Sequence Data; OVIDUCTE; OVIDUCTOS; Oviducts - metabolism; Peptide Fragments - chemistry; Peptide Fragments - isolation & purification; POLLO; POULET; PROTEINAS; PROTEINAS AGLUTINANTES; PROTEINE; PROTEINE DE LIAISON; Sequence Homology, Amino Acid; STRESS THERMIQUE; Transferrin-Binding Proteins
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1994.1414

A previously described transferrin binding protein from chicken oviduct has been identified as a heat shock protein, HSP108, by microsequencing of RP-HPLC purified tryptic peptides. The protein purified from oviduct by SDS-PAGE or from liver by ovotransferrin-affinity chromatography reacts with a monoclonal antibody raised against HSP108. The cDNA sequence predicts a KDEL peptide at the carboxyl terminus, but the protein does not react with anti-KDEL monoclonal antibodies, suggesting that HSP108 is processed in a way that eliminates the KDEL epitope.