title: Characterization of N-terminal amino acid sequence of monoclonal nonspecific suppressor factor.
abstract: Monoclonal nonspecific suppressor factor (MNSF), a product of a murine T cell hybridoma, suppresses the antibody response to lipopolysaccharide. In an attempt to clarify the N-terminal sequence, MNSF was prepared and purified by affinity chromatography with the use of an anti-MNSF monoclonal antibody (MO6), and reverse-phase high-pressure liquid chromatography. On the SDS-PAGE, the purified MNSF showed a single band with a molecular weight of 12,000. The N-terminal amino acid sequence of the protein was determined and showed no strong homology to any of the sequences of known biologically active proteins. However, the sequence revealed significant (60%) amino acid identity to transforming growth factor beta 2 (TGF beta 2).
authors.affiliation: Third Division of Internal Medicine, Shimane Medical University, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Nakamura
authors.forename: H
authors.initials: H
authors.lastname: Ogawa
authors.forename: T
authors.initials: T
authors.lastname: Tsunematsu
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D016415:Sequence Alignment; D013491:Suppressor Factors, Immunologic / Q000737:chemistry*
chemical_list: D013491:Suppressor Factors, Immunologic; C072169:monoclonal nonspecific suppressor factor