Fractionation and characterization of an amidated thermal 1:1:1-proteinoid

Abstract

1. 1.|Earlier studies indicating sharply limited heterogeneity in thermal proteinoids (polyanhydro-α-amino acids containing some proportion of each amino acid common to protein) have been extended. For this purpose, another type of proteinoid has been amidated and the resultant polymer fractionated on DEAE-cellulose. Six relatively symmetrical major peaks were obtained. After further purification, only small compositional differences between three of the fractions and the crude polymer were found in amino acid analyses. 2. 2.|The three fractions studied were individually examined further for heterogeneity by Sephadex exclusion and Bio-Gel exclusion, by high-voltage electrophoresis, and by ultracentrifugal analysis. The total results and related inferences are interpreted to signify a high degree of compositional uniformity throughout the original polymer. 3. 3.|Partial hydrolyzates of the three purified fractions yield ‘fingerprints’ which are similar and which contain 39–41 peaks in chromatograms. When viewed in the light of the compositional uniformity and earlier results indicating spontaneous ordering of residues in the synthesis of proteinoids, a high degree of sequential uniformity in the total polymer is suggested. 4. 4.|The significance of these results in the context of evolution of protein molecules is discussed.