pituitrin and 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

pituitrin has been researched along with 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate* in 1 studies

Other Studies

1 other study(ies) available for pituitrin and 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate

Article	Year
Partial characterization and solubilization of receptors for atrial natriuretic factor in rat glomeruli. Biochemical and biophysical research communications, 1985, Oct-30, Volume: 132, Issue:2 Specific receptors for atrial natriuretic factor (ANF) have been identified and solubilized in glomeruli from rat kidney. Radioiodinated synthetic ANF (Arg 101-Tyr 126) bound to a single class of high affinity (Kd 27 +/- 24 pM) sites with a density of 390 +/- 230 fmole/mg protein. The binding was time- and temperature-dependent, saturable and reversible. The ANF-receptor complex was not affected by angiotensin II, ACTH or vasopressin. Solubilization with 10 mM 3-[(3-cholamidopropyl)-dimethylammonio]- 1-propane sulfonate (CHAPS) slightly increased the affinity for ANF (Kd 5.0 +/- 3.3 pM) without affecting the density (250 +/- 110 fmole/mg protein). Similar results were found with 1% Triton X-100. ANF-related peptides interact generally in the same way with non-solubilized and solubilized receptors, indicating a fully preserved specificity of the receptors. Topics: Adrenocorticotropic Hormone; Angiotensin II; Animals; Atrial Natriuretic Factor; Cholic Acids; Detergents; Kidney Glomerulus; Membrane Proteins; Octoxynol; Polyethylene Glycols; Rats; Receptors, Atrial Natriuretic Factor; Receptors, Cell Surface; Solubility; Vasopressins	1985

Article

Year

Partial characterization and solubilization of receptors for atrial natriuretic factor in rat glomeruli.

Biochemical and biophysical research communications, 1985, Oct-30, Volume: 132, Issue:2

Specific receptors for atrial natriuretic factor (ANF) have been identified and solubilized in glomeruli from rat kidney. Radioiodinated synthetic ANF (Arg 101-Tyr 126) bound to a single class of high affinity (Kd 27 +/- 24 pM) sites with a density of 390 +/- 230 fmole/mg protein. The binding was time- and temperature-dependent, saturable and reversible. The ANF-receptor complex was not affected by angiotensin II, ACTH or vasopressin. Solubilization with 10 mM 3-[(3-cholamidopropyl)-dimethylammonio]- 1-propane sulfonate (CHAPS) slightly increased the affinity for ANF (Kd 5.0 +/- 3.3 pM) without affecting the density (250 +/- 110 fmole/mg protein). Similar results were found with 1% Triton X-100. ANF-related peptides interact generally in the same way with non-solubilized and solubilized receptors, indicating a fully preserved specificity of the receptors.

Topics: Adrenocorticotropic Hormone; Angiotensin II; Animals; Atrial Natriuretic Factor; Cholic Acids; Detergents; Kidney Glomerulus; Membrane Proteins; Octoxynol; Polyethylene Glycols; Rats; Receptors, Atrial Natriuretic Factor; Receptors, Cell Surface; Solubility; Vasopressins

1985