Abstract
Aliphatic amines of increasing chainlength (butyl, capryl, lauryl, and palmityl) and increasing degree of unsaturation (stearyl, oleyl, and linoleyl) were bound by amide bonds to polyacrylic acid resin. Mitochondrial membrane proteins solubilized with cholate and deoxycholate were chromatographically separated on such resins.The separation efficiency as measured by the number of protein fractions and their specific cytochrome content was highest with capryl or linoleyl resins while the free polyacrylic acid resin or the stearyl resin proved to be the most ineffective ones.These effects are discussed in terms of free thermal mobility of the aliphatic chains necessary for hydrophobic interaction with the membrane proteins.
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