Purification of the insulin receptor from human placental membranes.
Insulin receptors were purified from human placental microsomal membranes by solubilisation with Triton X-100 followed by Sepharose 6B chromatography, phosphate gradient elution from hydroxyapatite and affinity chromatography on concanavalin A-Sepharose. 2000-fold purification was achieved with 63% overall recovery. The purified receptor gave a single band on 3.75% polyacrylamide (0.1% Triton X-100) gel electrophoresis. On sodium dodecyl sulphate-polyacrylamide gel electrophoresis there was a major band at 75,000 and a minor band at 80,000 daltons. The purified receptor rechromatographed on Sepharose 6B with an apparent molecular weight of 300,000.
D005260:Female; D006801:Humans; D007425:Intracellular Membranes / Q000032:analysis; D008722:Methods; D008861:Microsomes / Q000032:analysis; D008970:Molecular Weight; D010920:Placenta / Q000032:analysis*; D011247:Pregnancy; D011972:Receptor, Insulin / Q000302:isolation & purification*
D011972:Receptor, Insulin