TY - JOUR
T1 - Analysis of ACTH-related and CLIP-related peptides partially purified from the pituitary of the Australian lungfish, Neoceratodus forsteri
AU - Dores, Robert M.
AU - Adamczyk, Darcy L.
AU - Joss, Jean M P
PY - 1990
Y1 - 1990
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0025289444&partnerID=8YFLogxK
U2 - 10.1016/0016-6480(90)90088-4
DO - 10.1016/0016-6480(90)90088-4
M3 - Article
C2 - 2162307
AN - SCOPUS:0025289444
SN - 0016-6480
VL - 79
SP - 64
EP - 73
JO - General and Comparative Endocrinology
JF - General and Comparative Endocrinology
IS - 1
ER -