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Isolation and identification of a polypeptide in the Hsp 70 family that binds substance P.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1990 Jan 30; Vol. 166 (2), pp. 978-83. - Publication Year :
- 1990
-
Abstract
- During the course of an attempt to purify the substance P (SP) receptor from horse salivary glands by substance P-affinity chromatography, a polypeptide of Mr = 78,000 was isolated. The first fifteen amino acid residues at the amino terminus were determined and, unexpectedly, were found to be identical with the amino terminus of a glucose-regulated protein (GRP) of the same molecular weight, a protein that has been identified as a member of the heat shock protein family. This finding raises the intriguing possibility that SP may interact in vivo with GRPs and other members of the heat shock protein family and play a role in modulating their biological activities.
- Subjects :
- Amino Acid Sequence
Animals
Carrier Proteins metabolism
Chromatography, Affinity
Heat-Shock Proteins metabolism
Horses
Molecular Sequence Data
Molecular Weight
Multigene Family
Submandibular Gland analysis
Carrier Proteins isolation & purification
Heat-Shock Proteins isolation & purification
Substance P metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 166
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 1689156
- Full Text :
- https://doi.org/10.1016/0006-291x(90)90907-5