Analysis of ACTH-related and CLIP-related peptides partially purified from the pituitary of the Australian lungfish, Neoceratodus forsteri

Robert M. Dores*, Darcy L. Adamczyk, Jean M P Joss

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    15 Citations (Scopus)

    Abstract

    Acid extracts of individual lungfish pituitaries were fractionated by gel filtration on a Sephadex G-75 column and aliquots of column fractions were screened with a heterologous ACTH(1-39) radioimmunoassay (RIA). Two major, incompletely separated, peaks of ACTH-related immunoreactivity were detected. These peaks of ACTH-related material were resolved by reverse-phase high-performance liquid chromatography and were designated Peak A and Peak B. Peak A had a retention time more hydrophilic than synthetic human CLIP [ACTH(18-39)], whereas Peak B had a retention time similar to, but not identical with, human ACTH(1-39). Further analysis indicated that Peak A had an apparent molecular weight of 2.5K and an isoelectric point of 4.3. Based on these characteristics, Peak A would appear to be lungfish CLIP. Peak B had an apparent molecular weight of 4.5K. Based on chromatographic and immunological properties, Peak B would appear to be lungfish ACTH. The detection of these lungfish peptides by heterologous RIA indicates a high degree of primary sequence homology between lungfish and tetrapod ACTH-related polypeptides.

    Original languageEnglish
    Pages (from-to)64-73
    Number of pages10
    JournalGeneral and Comparative Endocrinology
    Volume79
    Issue number1
    DOIs
    Publication statusPublished - 1990

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