Improved technique for the analysis of amino acids and  related compounds  on thin layers of cellulose.XI. Direct, visual micro-method for investigating the primary structural sequence of collagen and other proteins.
The present paper describes a new variation of the "finger printing" technique for examining the primary structure of proteins. It is based on the production of a reproducible, partial acid hydrolysate consisting of amino acids and small peptides which are separated into compact spots by bi-dimensional thin-layer chromatography. The spots are characterized by ther Rf values and colour reactions with a variety of reagents. The method was initially developed for collagen but has been applied to other proteins, with interesting results. It has developed logically from earlier, systematic studies on amino acids and peptides, and holds promise for the comparative investigation of normal and diseased human collagen.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002417:Cattle; D002482:Cellulose; D002855:Chromatography, Thin Layer / Q000379:methods*; D003094:Collagen / Q000032:analysis*; D003124:Colorimetry; D005934:Glucagon; D006801:Humans; D008832:Microchemistry; D010455:Peptides / Q000032:analysis; D011492:Protein Hydrolysates / Q000032:analysis; D011506:Proteins / Q000032:analysis
D000596:Amino Acids; D010455:Peptides; D011492:Protein Hydrolysates; D011506:Proteins; D002482:Cellulose; D003094:Collagen; D005934:Glucagon