On the Electrophoretic Behavior of Thermal Polymers of Amino Acids
The limited heterogeneity of anumber of thermal polymers of amino acids, also called proteinoids (1), has been established in several reports (2–8). Particularly, if the polymers were subjected to electrophoretic analysis they could be separated into only a small number of definable fractions, mostly three or less. Often electrophoresis even signified true-near-homogeneity. In some instances the single fraction appeared to have a higher degree of homogeneity than even purified organismic proteins. Examples are the acrylamide gel electrophoresis of an unfractionated, but amidated 1:1:1* proteinoid (8) and the gel electrophoresis of a hemoproteinoid (molecular weight about 18.000) which possesses peroxidase-like activity (6–7). However, substantial evidence indicates that electrophoreses is inferior in sensitivity to fractionation on DEAE-Sephadex, DEAE-cellulose, and other cellulose ion exchangers. Fox and Nakashima (8) separated on DEAE-cellulose the amidated 1:1:1 proteinoid into at least three major fractions which all showed identical electrophoretical mobilities. A number of related results which have been obtained in our laboratory are published here.
KeywordsAspartic Acid Amino Acid Composition Cellulose Acetate Ammonium Sulfate Amino Acid Mixture
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