Abstract
Membrane protein from the lateral geniculate bodies and superior colliculi of the rabbit brain was subjected to sequential solubilization with various solvents. The solubilization media was: EDTA at low ionic strength, 1 M NaCl, chloroform-methanol, 6 M urea, lithium diiodosalycylate and sodium dodecyl sulphate. Each solubilized fraction was subjected to electrophoresis in the presence of dodecyl sulphate in order to study its polypeptide composition. It was found that treatment with EDTA, NaCl and urea could solubilize about 40 per cent of the membrane proteins. A large number of polypeptides was found among the EDTA and NaCl soluble proteins. Urea solubilized preferentially a polypeptide with a mol. wt. of 22,000. Lithium diiodosalicylate solubilized a polypeptide with a mol. wt. of 52,000. The remaining membrane fraction, which was solubilized with dodecyl sulphate, showed a complex polypeptide composition. The dominating polypeptides had mol. wts. of 22,000, 52,000 and 95,000.
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