Distinct alpha-subunit structures of human insulin receptor A and B variants determine differences in tyrosine kinase activities.

doi:10.1021/bi00134a008

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Article

Distinct alpha-subunit structures of human insulin receptor A and B variants determine differences in tyrosine kinase activities.

Biochemistry - 19 May 1992

Kellerer M, Lammers R, Ermel B, Tippmer S, Vogt B, Obermaier-Kusser B, Ullrich A, Häring H U

Abstract excerpt

Human insulin receptor isoforms (HIR-A and -B) differ in their alpha-subunit structures which result from alternatively spliced precursor mRNAs. This structural difference causes distinct binding affinities for insulin. To determine the impact of the structural difference on receptor signaling, we characterized the tyrosine kinase activity of HIR-A and HIR-B in vitro and determined the insulin stimulated...

Topics

Animals
Cells, Cultured
Chromatography, High Pressure Liquid
Enzyme Activation
Fibroblasts
Genetic Variation
Humans
Insulin
Kinetics
Peptide Fragments
Peptide Mapping

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Phosphorylation

Phosphotyrosine

Precipitin Tests

Protein Binding

Protein-Tyrosine Kinases

Rats

Receptor, Insulin

Source

Open in PubMed

Identifiers

PMID: 1374639
DOI: 10.1021/bi00134a008

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1374639-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

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

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