Differences in binding affinities of human PTH(1-84) do not alter biological potency: a comparison between chemically synthesized hormone, natural and mutant forms.

doi:10.1016/0196-9781(94)90151-1

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Article

Differences in binding affinities of human PTH(1-84) do not alter biological potency: a comparison between chemically synthesized hormone, natural and mutant forms.

Peptides - 1 Jan 1994

Olstad O K, Morrison N E, Jemtland R, Jüppner H, Segre G V, Gautvik K M

Abstract excerpt

The purpose of this study was to evaluate receptor binding affinities and biological properties in vitro and in vivo of various recombinant hPTH(1-84) forms representing the natural hormone and a mutagenized hPTH form, [Gln26]hPTH(1-84) (QPTH), after expression in E. coli and Saccharomyces cerevisiae. In LLC-PK1 cells stably transformed with the rat PTH/PTHrP receptor, chemically synthesized hPTH(1-84) and QPTH...

Topics

Animals
Cyclic AMP
Escherichia coli
Humans
Hypercalcemia
In Vitro Techniques
Kinetics
LLC-PK1 Cells
Male
Mutation
Parathyroid Hormone

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Radioligand Assay

Rats

Rats, Wistar

Receptors, Parathyroid Hormone

Recombinant Proteins

Saccharomyces cerevisiae

Swine

Source

Open in PubMed

Identifiers

PMID: 7854979
DOI: 10.1016/0196-9781(94)90151-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7854979-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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