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Scientific article
English

Functional Activity of a Biotinylated Human Neurokinin 1 Receptor Fusion Expressed in the Semliki Forest Virus System

Published inBiochemical and biophysical research communications, vol. 208, no. 1, p. 260-266
Publication date1995
Abstract

The 1.3 S biotinylatable subunit of Proprionibacterium shermanii transcarboxylase complex was fused to the C-terminus of the human neurokinin 1 receptor gene and introduced into the Semliki Forest virus expression vector pSFV1. RNA transcribed from pSFV1-NK1-biot and pSFV-Helper2 was coelectroporated into BHK cells permitting in vivo packaging of recombinant virus. Infection of BHK and CHO cells with SFV-NK1-biot virus yielded high level of the fusion receptor as detected by metabolic labeling, immunoblotting with streptavidin alkaline phosphatase and binding to substance P. Like native receptor, the biotinylated receptor fusion was able to stimulate Ca2+ mobilization in infected CHO cells,indicating functional coupling to guanine-nucleotide-binding proteins.

Keywords
  • Hamster ovary cells
  • Escherichia-coli
  • Substance-P
  • Peptides
  • Binding
  • Protein
  • Vectors
Research group
Citation (ISO format)
LUNDSTROM, Kenneth, VARGAS, Alfredo, ALLET, Bernard. Functional Activity of a Biotinylated Human Neurokinin 1 Receptor Fusion Expressed in the Semliki Forest Virus System. In: Biochemical and biophysical research communications, 1995, vol. 208, n° 1, p. 260–266. doi: 10.1006/bbrc.1995.1332

Technical informations

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