A HIGHLY IMMUNOREACTIVE PEPTIDE FRAGMENT OF HUMAN LUTEINIZING HORMONE ALPHA SUBUNIT, DISCERNED WITH A NEW, “SEQUENCE-SPECIFIC” RADIOIMMUNOASSAY
- 1 July 1975
- journal article
- other
- Published by The Endocrine Society in Journal of Clinical Endocrinology & Metabolism
- Vol. 41 (1) , 195-198
- https://doi.org/10.1210/jcem-41-1-195
Abstract
HLHα, WHOSE PRIMARY AMINO ACID SEQUENCE IS KNOWN, WAS REDUCED AND S-CARBOXYMETHYLATED (RCM) TO REMOVE SECONDARY AND TERTIARY STRUCTURE. RCM-hLHα WAS UTILIZED FOR DEVELOPMENT OF A “SEQUENCE SPECIFIC” RIA. RCM-hLHα RIA REVEALED THAT THE NH2-TERMINAL TRYPTIC PEPTIDE OF hLHα (CONSISTING OF ONLY 32 AMINO ACID RESIDUES) WAS NEARLY AS IMMUNOREACTIVE AS THE ENTIRE RCM-hLHα MOLECULE (CONSISTING OF 89 RESIDUES). NO OTHER TRYPTIC PEPTIDE WAS IMMUNOACTIVE. REDUCED AND S-CARBAMIDOMETHYLATED hLHα, DIFFERING ONLY SLIGHTLY IN STRUCTURE FROM RCM-hLHα, WAS WEAKLY ACTIVE IN THE RCM-hLHα RIA, DEMONSTRATING THE UTILITY OF THIS RIA FOR PRECISE STUDY OF STRUCTURE-IMMUNOLOGIC ACTIVITY RELATIONSHIPS.Keywords
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