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Journal of Clinical Endocrinology & Metabolism, Vol 41, 195-198, Copyright © 1975 by Endocrine Society

ARTICLES

A highly immunoreactive peptide fragment of human luteinizing hormone alpha subunit, discerned with a new, "sequence-specific" radioimmunoassay

AF Parlow and B Shome

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.




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Copyright © 1975 by The Endocrine Society