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DEVELOPMENT OF A RADIOIMMUNOASSAY FOR AN AMINO‐TERMINAL PEPTIDE OF PRO‐OPIOCORTIN CONTAINING THE γ‐MSH REGION: MEASUREMENT AND CHARACTERIZATION IN HUMAN PLASMA
Author(s) -
HOPE J.,
RATTER SALLY J.,
ESTIVARIZ F. E.,
McLOUGHLIN LORRAINE,
LOWRY P. J.
Publication year - 1981
Publication title -
clinical endocrinology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.055
H-Index - 147
eISSN - 1365-2265
pISSN - 0300-0664
DOI - 10.1111/j.1365-2265.1981.tb00658.x
Subject(s) - radioimmunoassay , endocrinology , human plasma , medicine , antiserum , peptide , glycoprotein , chemistry , molecular mass , amino acid residue , amino acid , peptide sequence , amino terminal , peptide hormone , pituitary gland , antibody , biology , chromatography , biochemistry , hormone , enzyme , immunology , gene
SUMMARY A radioimmunoassay has been developed for the N‐terminal region of human pituitary pro‐opiocortin (N‐POC), the common precursor protein of ACTH and β‐LPH, using an antiserum which recognizes residues near the γ‐MSH region. The concentrations of greater than 300 ng/l of immunoreactive peptide were determined in unextracted human plasma, the relative molecular mass of the reacting fragments corresponding to a seventy‐seven amino acid glycoprotein. The concentrations of immunoreactive N‐POC peptides were correlated with those of ACTH in plasma obtained from patients with various disorders of the hypothalamic‐pituitary‐adrenal axis.