A highly immunoreactive peptide fragment of human luteinizing hormone alpha subunit, discerned with a new, "sequence-specific" radioimmunoassay.
hLHa, whose primary amino acid sequence is known, was reduced and s-carboxymethylated (RCM) to remove secondary and teriary structure. RCM-hLHa was utilized for development of a "sequence specific" ria. RCM-hLHa ria revealed that the NH2-terminal tryptic peptide of hLHa (consisting of only 32 amino acid residues) was nearly as immunoreactive as the entire RCM-hLHa molecule (consisting of 89 residues). No other tryptic peptide was immunoactive. Reduced and s-carbamidomethylated hLHa, differing only slight in structure from RCM-hLHa, was weakly active in the RCM-hLHa ria, demonstrating the utility of this ria for precise study of structure-immunologic activity relationships.
D000478:Alkylation; D000818:Animals; D002852:Chromatography, Ion Exchange; D006168:Guinea Pigs / Q000276:immunology; D006801:Humans; D007986:Luteinizing Hormone / Q000032:analysis*; D046911:Macromolecular Substances; D008722:Methods; D010084:Oxidation-Reduction; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification; D011863:Radioimmunoassay; D013329:Structure-Activity Relationship; D014357:Trypsin
D046911:Macromolecular Substances; D010455:Peptides; D007986:Luteinizing Hormone; D014357:Trypsin