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A HIGHLY IMMUNOREACTIVE PEPTIDE FRAGMENT OF HUMAN LUTEINIZING HORMONE ALPHA SUBUNIT, DISCERNED WITH A NEW, "SEQUENCE-SPECIFIC" RADIOIMMUNOASSAY

DEPARTMENT OF OBSTETRICS AND GYNECOLOGY, HARBOR GENERAL HOSPITAL CAMPUS OF THE UCLA SCHOOL OF MEDICINE TORRANCE, CALIFORNIA 90509

hLH, WHOSE PRIMARY AMINO ACID SEQUENCE IS KNOWN, WAS REDUCED AND S-CARBOXYMETHYLATED (RCM) TO REMOVE SECONDARY AND TERTIARY STRUCTURE. RCM-hLH WAS UTILIZED FOR DEVELOPMENT OF A "SEQUENCE SPECIFIC" RIA. RCM-hLH RIA REVEALED THAT THE NH₂-TERMINAL TRYPTIC PEPTIDE OF hLH (CONSISTING OF ONLY 32 AMINO ACID RESIDUES) WAS NEARLY AS IMMUNOREACTIVE AS THE ENTIRE RCM-hLH MOLECULE (CONSISTING OF 89 RESIDUES). NO OTHER TRYPTIC PEPTIDE WAS IMMUNOACTIVE. REDUCED AND S-CARBAMIDOMETHYLATED hLH, DIFFERING ONLY SLIGHTLY IN STRUCTURE FROM RCM-hLH, WAS WEAKLY ACTIVE IN THE RCM-hLH RIA, DEMONSTRATING THE UTILITY OF THIS RIA FOR PRECISE STUDY OF STRUCTURE-IMMUNOLOGIC ACTIVITY RELATIONSHIPS.