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- W1986218086 abstract "PTH-like protein-(1–74) [PTHLP-(l–74)] was synthesized and purified. On the basis of chromatographic criteria and amino acid composition of the full-length peptide, direct amino acid sequencing of the N-terminus, and amino acid composition and internal sequence of proteolytic fragments of PTHLP-(1-74), the synthetic peptide appears to be of high quality and purity. Physiological comparison of PTHLP-(l–74) to [Tyr36]- PTHLP-(l-36) amide and bovine (b) PTH-(l-34) indicates that all three peptides are of equivalent potency in the fetal rat long bone and rat osteosarcoma 17/2.8 adenylate cyclase assays. However, as in earlier studies with native and N-terminal PTHLPs, PTHLP-(l–74) is considerably less potent (2%) in stimulating the canine renal cortical adenylate cyclase assay than is bPTH-(l-34). Further, PTHLP-(l–74) displayed only 12% of the activity of bPTH-(l-34) in inducing hypercalcemia when infused into rats in vivo. These studies support the possibility that subclasses of PTH receptors or varying PTH- and PTHLP-signalling transduction mechanisms may exist. In addition, they emphasize the need to precisely define the naturally occurring secretory and circulating species of this novel class of peptide hormones. (Endocrinology124: 642–648, 1989)" @default.
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- W1986218086 date "1989-02-01" @default.
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- W1986218086 title "Synthetic Parathyroid Hormone-Like Protein-(1–74): Biochemical and Physiological Characterization*" @default.
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- W1986218086 doi "https://doi.org/10.1210/endo-124-2-642" @default.
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