Solubilization of Membrane-Bound Enzymes

From an operational viewpoint, there is a spectrum of proteins associated with membranes. At one end of the spectrum are those proteins such as erythrocyte glyceraldehyde-3-phosphate dehydrogenase (G-3-PD) that appear to be bound to the membrane through coulombic forces and which are released under conditions utilizing changes in ionic strength. Beyond this, one encounters the vast majority of membrane-bound proteins which interact with both the hydrophilic and hydrophobic domains of the membrane, while at the other end of the spectrum lie those proteins located entirely within the hydrocarbon core of the membrane. This wide spectrum dictates careful selection 

Low ionic strength, very Removes adsorbed proteins-such enzymes Maddy and Dunn 

High ionic strength Extracts 30-40% of red cell protein acetylcholinesterase Maddy and Dunn (1976) 

Chaotropic agents (SCN and ClOr Extracts complex I from mitochondria Hatefi and Hanstein (1974) 

Organic solvents Succinate DH and coupling factor F2 solubilized Beechey and Cattell (1973) 

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