Identification and solubilization of atrial natriuretic factor receptors in human placenta.
Specific high affinity 125I-atrial natriuretic factor binding sites have been identified in human placental membranes. Using the nonionic detergent, Triton X-100, these binding sites were quantitatively solubilized and retained binding activity. In the solubilized preparation, the macromolecular component that binds atrial natriuretic factor is a 160,000 dalton protein as shown by covalently cross-linking it to 125I-atrial natriuretic factor with the bifunctional chemical crosslinker, disuccinimidyl suberate, followed by gel electrophoresis and autoradiography. On Sephadex G-200 gel filtration in the presence of detergent, the hormone-receptor complex elutes in the molecular weight range of 140,000. These observations suggest strongly that a 140- 160,000 dalton protein present in human placental membranes is the receptor for specific recognition of atrial natriuretic factor.
D009320:Atrial Natriuretic Factor; D002850:Chromatography, Gel; D003432:Cross-Linking Reagents; D005260:Female; D006801:Humans; D008970:Molecular Weight; D017830:Octoxynol; D010920:Placenta / Q000378:metabolism*; D011092:Polyethylene Glycols; D011247:Pregnancy; D017461:Receptors, Atrial Natriuretic Factor; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D012995:Solubility; D013388:Succinimides
D003432:Cross-Linking Reagents; C472955:NPPA protein, human; D011956:Receptors, Cell Surface; D013388:Succinimides; D011092:Polyethylene Glycols; D009320:Atrial Natriuretic Factor; D017830:Octoxynol; D017461:Receptors, Atrial Natriuretic Factor; C019358:disuccinimidyl suberate