2. Academic Validation
  3. Analysis of ACTH-related and CLIP-related peptides partially purified from the pituitary of the Australian lungfish, Neoceratodus forsteri

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

  • Gen Comp Endocrinol. 1990 Jul;79(1):64-73. doi: 10.1016/0016-6480(90)90088-4.
R M Dores 1,  D L Adamczyk,  J M Joss
Affiliations

Affiliation

  • 1 University of Denver, Department of Biological Sciences, Colorado 80208.
PMID: 2162307 DOI: 10.1016/0016-6480(90)90088-4
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.

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