Purification and subunit composition of atrial natriuretic peptide receptor

Journal Article · Sun Mar 01 00:00:00 EST 1987 · Proc. Natl. Acad. Sci. U.S.A.; (United States)

DOI:https://doi.org/10.1073/pnas.84.6.1521· OSTI ID:6526167

Schenk, D B; Phelps, M N; Porter, J G; Fuller, F; Cordell, B; Lewicki, J A

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 NaDodSO/sub 4//polyacrylamide gel electrophoresis. With /sup 125/I-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 NaDodSO/sub 4//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).

• Research Organization: California Biotechnology, Inc., Mountain View, CA
• OSTI ID: 6526167
• Journal Information: Proc. Natl. Acad. Sci. U.S.A.; (United States), Vol. 6
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
PEPTIDES
RECEPTORS
CHEMICAL COMPOSITION
FRACTIONATION
AORTA
CATTLE
ELECTROPHORESIS
IODINE 125
LIGANDS
MOLECULAR WEIGHT
MUSCLES
TRACER TECHNIQUES
ANIMALS
ARTERIES
BETA DECAY RADIOISOTOPES
BLOOD VESSELS
BODY
CARDIOVASCULAR SYSTEM
DAYS LIVING RADIOISOTOPES
DOMESTIC ANIMALS
ELECTRON CAPTURE RADIOISOTOPES
INTERMEDIATE MASS NUCLEI
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
MAMMALS
MEMBRANE PROTEINS
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANS
PROTEINS
RADIOISOTOPES
RUMINANTS
SEPARATION PROCESSES
VERTEBRATES
550201* - Biochemistry- Tracer Techniques