Synthesis and biological activity of four gamma-melanotropin peptides derived from the cryuptic region of the adrenocorticotropin/beta-lipotropin precursor. |
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Authors: | N Ling S Ying S Minick R Guillemin |
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Affiliation: | Laboratories for Neuroendocrinology The Salk Institute for Biological Studies La Jolla, California 92037, USA |
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Abstract: | A third melanotropin coding fragment named γ-MSH was discovered by Nakanishi et al (Nature , 423–427 (1979)) in the cryptic region outside the portion coding for ACTH and β-LPH in the ACTH/β-LPH precursor mRNA isolated from the intermediate lobe of bovine pituitary. Four possible γ-MSH peptides derived from this coding fragment were synthesized by solid-phase methodology and their bioactivity determined in an MSH assay as well as the anterior pituitary primary culture assay. Relative to α-MSH, the melanotropic activities of Ac-γ1-MSH, γ1-MSH, γ2-MSH and γ3-MSH are 7.3 × 10?4, 3.3 × 10?5, 1.4 × 10?4 and 4.6 × 10?7 respectively. None of these γ-MSH peptides releases LH, FSH, PRL, GH and TSH in the pituitary culture medium at a dose as high as 100 ng per dish. |
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