Functional characterization of the in vitro folded human y(1) receptor in lipid environment

S Schimmer; D Lindner; P Schmidt; A G Beck-Sickinger; D Huster; R Rudolph

doi:10.2174/092986610791112783

Functional characterization of the in vitro folded human y(1) receptor in lipid environment

Protein Pept Lett. 2010 May;17(5):605-9. doi: 10.2174/092986610791112783.

Authors

S Schimmer¹, D Lindner, P Schmidt, A G Beck-Sickinger, D Huster, R Rudolph

Affiliation

¹ Institute of Biochemistry/Biotechnology, Martin Luther University Halle-Wittenberg, Germany.

PMID: 19689227
DOI: 10.2174/092986610791112783

Abstract

We describe the recombinant production of the human Y(1) receptor from inclusion bodies of E. coli cultures. The in vitro refolding was carried out in the presence of lipids from bovine brain extracts. Y(1) receptors in brain lipids compete for cellular receptors in competitive binding experiments.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Animals
Binding, Competitive
Brain Chemistry
Cattle
Cell Line, Tumor
Escherichia coli / genetics
Humans
Membrane Lipids / metabolism*
Neuroblastoma
Neuropeptide Y / metabolism
Phosphorus Isotopes
Protein Folding
Receptors, Neuropeptide Y / chemistry
Receptors, Neuropeptide Y / genetics
Receptors, Neuropeptide Y / metabolism*
Recombinant Proteins / chemistry
Recombinant Proteins / genetics
Recombinant Proteins / metabolism*
Swine
Tritium

Substances

Membrane Lipids
Neuropeptide Y
Phosphorus Isotopes
Receptors, Neuropeptide Y
Recombinant Proteins
Tritium