Add time:07/18/2019 Source:sciencedirect.com
1.1. The biologic activity of bovine 8,18-norleucine 34-tyrosine parathyroid hormone (1–34) amide [norleu PTH (1–34)] was compared to the native sequence of bovine parathyroid hormone [PTH (1–34)] in chicken kidney and bone in in vitro assay systems.2.2. The analogue was a full agonist, but was less potent than the native sequence in stimulating cyclic AMP formation by renal slices or embryonic tibiae.3.3. Norleu PTH was less potent and did not achieve the maximal velocity produced by PTH (1–34) in renal membrane adenylate cyclase activity.4.4. When guanylimidodiphosphate was added to the adenylate cyclase assays, the same maximal activation was achieved by both peptides, but the difference in potency was not altered.5.5. Renal membrane receptor binding assays indicated that the norleucine analogue did not compete as well as native bovine PTH for specific membrane receptor sites.6.6. The results of these comparisons indicate that the differences in efficacy found in the adenylate cyclase assay reflect coupling of the hormone-receptor complex to the catalytic subunit of the enzyme while the differences in potency reflect hormone-receptor interactions.
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