Abstract
A receptor for atrial natriuretic peptide (ANP) was purified 2700-fold, to apparent homogeneity, from cultured bovine aortic smooth muscle cells by affinity chromatography. The native ANP receptor has a molecular weight of 125,000 as determined by both metrizamide gradient centrifugation and nonreducing NaDodSO4/polyacrylamide gel electrophoresis. With 125I-labeled ANP as ligand, the purified receptor bound a maximum of 5.70 nmol of ligand per mg of protein and the dissociation constant was 4.0 X 10(-10)M. Upon treatment with 10 mM dithiothreitol, the purified receptor migrated as a single band at Mr 60,500 in NaDodSO4/polyacrylamide gel electrophoresis. These findings show that the holoreceptor for ANP in vascular tissue is composed of two subunits of identical apparent molecular weight, presumably linked by a disulfide bridge(s).
Dates
Type | When |
---|---|
Created | 19 years, 3 months ago (May 31, 2006, 3:57 a.m.) |
Deposited | 3 years, 4 months ago (April 13, 2022, 12:26 p.m.) |
Indexed | 11 months, 3 weeks ago (Sept. 6, 2024, 8:24 a.m.) |
Issued | 38 years, 6 months ago (March 1, 1987) |
Published | 38 years, 6 months ago (March 1, 1987) |
Published Online | 38 years, 6 months ago (March 1, 1987) |
Published Print | 38 years, 6 months ago (March 1, 1987) |
@article{Schenk_1987, title={Purification and subunit composition of atrial natriuretic peptide receptor.}, volume={84}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.84.6.1521}, DOI={10.1073/pnas.84.6.1521}, number={6}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Schenk, D B and Phelps, M N and Porter, J G and Fuller, F and Cordell, B and Lewicki, J A}, year={1987}, month=mar, pages={1521–1525} }