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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Solubilization and characterization of active somatostatin receptors from rat pancreas.

Somatostatin receptors were solubilized from rat pancreatic membranes with the zwitterionic detergent 3-[(3-cholamidopropyl)dimethylammonio]-1-propane-sulfonic acid (CHAPS). The binding of an iodinated somatostatin analog [125I-Tyr3]SMS to the soluble fraction was time-dependent, saturable, and reversible. Scatchard analysis of equilibrium binding data indicated that the soluble extract contained a single class of somatostatin binding sites with a Kd of 0.3 nM and a Bmax of 210 fmol/mg. As observed with membrane-bound receptors, soluble binding receptors were sensitive to the GTP analog GTP gamma S indicating that they are functionally linked to a G protein. A molecular weight of about 400,000 was determined for soluble receptors under native conditions by gel filtration. In denaturing gel electrophoresis, photoaffinity labeling of soluble receptors identified a major protein of Mr = 100,000 and two minor proteins of Mr = 56,000 and 21,000. Isoelectric focusing of soluble receptors revealed that the somatostatin receptor is an acidic protein with pI 4. 8. The soluble somatostatin receptor is a glycoprotein which can be specifically bound to the wheat germ agglutinin lectin and eluted by triacetyl-chitotriose.[1]

References

  1. Solubilization and characterization of active somatostatin receptors from rat pancreas. Knuhtsen, S., Esteve, J.P., Cambillau, C., Colas, B., Susini, C., Vaysse, N. J. Biol. Chem. (1990) [Pubmed]
 
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