SELECTIVE EFFECTS OF NONIONIC DETERGENT AND SALT-SOLUTIONS IN DISSOLVING NUCLEAR-ENVELOPE PROTEIN

Protein was selectively extracted from isolated chicken erythrocyte nuclear envelope by dilute MgCl2/Triton X-100 followed by concentrated MgCl2/Trition X-100 solutions. Certain proteins appear to be selectively dissolved in the 1st solvent and may occur in the nuclear envelope primarily as lipoproteins. Among the proteins insoluble in the low MgCl2/Triton X-100 wash, as well as in 500 mM MgCl2 without Triton previously used in the preparation of the envelope fraction, the quantitatively major polypeptides dissolve in a combination of high MgCl2 and Triton X-100. Much of this dissolved protein precipitates when the MgCl2 concentration is lowered by dialysis. The insolubility of these proteins appears to result from a combination of ionic and hydrophobic interactions and may explain the resistance of nuclei to various manipulative procedures including nonionic detergent washes. The procedures described provide a route for gently and selectively dissolving representative proteins from the nuclear envelope lipoprotein matrix and from the envelope residual protein.