Characterization of a synthetic peptide corresponding to a receptor binding domain of mouse interferon .gamma

• Published in: Biochemistry (Easton) Vol. 30; no. 23; pp. 5784 - 5789
• Main Authors: Magazine, Harold I, Johnson, Howard M
• Format: Journal Article
• Language: English
• Published: United States American Chemical Society 11.06.1991
• Subjects: 550201 - Biochemistry- Tracer Techniques; Amino Acid Sequence; Animals; ANTIBODIES; BASIC BIOLOGICAL SCIENCES; BETA DECAY RADIOISOTOPES; Binding, Competitive; Cattle; Circular Dichroism; DAYS LIVING RADIOISOTOPES; DICHROISM; ELECTRON CAPTURE RADIOISOTOPES; GLYCOPROTEINS; GROWTH FACTORS; Humans; INTERFERON; Interferon-gamma - chemistry; Interferon-gamma - metabolism; INTERMEDIATE MASS NUCLEI; INTERNAL CONVERSION RADIOISOTOPES; IODINE 125; IODINE ISOTOPES; ISOTOPES; LYMPHOKINES; MAGNETIC CIRCULAR DICHROISM; MEMBRANE PROTEINS; Mice; MITOGENS; Molecular Sequence Data; MONOCLONAL ANTIBODIES; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; Peptide Fragments - chemistry; Peptide Fragments - metabolism; PEPTIDES; Protein Conformation; PROTEINS; RADIOISOTOPES; Rats; RECEPTORS; Receptors, Immunologic - chemistry; Receptors, Immunologic - metabolism; Receptors, Interferon; SPECTRA; Structure-Activity Relationship; ULTRAVIOLET SPECTRA

A receptor binding region of mouse interferon gamma (IFN gamma) has previously been localized to the N-terminal 39 amino acids of the molecule by use of synthetic peptides and monoclonal antibodies. In this report, a detailed analysis of the synthetic peptide corresponding to this region, IFN gamma...