An accelerated step-gradient procedure for the automatic analysis of collagen hydrolyzates

✍ Scribed by Roy C. Page; David Jones; Ronald Hansen

• Publisher: Elsevier Science
• Year: 1970
• Tongue: English
• Weight: 319 KB
• Volume: 37
• Category: Article
• ISSN: 0003-2697
• DOI: 10.1016/0003-2697(70)90051-5

✦ Synopsis

Since the advent of automated procedures, amino acid analysis has become a routine and integral part of the analytical procedures used by the protein chemist. This procedure has been particularly fruitful in the study of the structure of collagen and elastin. Most analytical systems for amino acid analysis are based either on the step-gradient procedure devised by Spackman, Stein, and Moore (1) or the single-column continuous-gradient system of Piez and Morris (2). Originally these systems required a day or more for complete hydrolyzate analysis, but recent advances have led to modifications in which complete analyses for most protein hydrolyzates can be done in 2 hr or less. Hydrolyzates of collagen and elastin present a special problem since they are more complex #than those of most other proteins, and it has not ,been possible to obtain satisfactory resolution of the components using the very short time periods. Miller and Piez (3) devised a modification of the continuous-gradient system in which these hydrolyzates can be adequately resolved in 260 min. However, this system does not permit use of the automated features of commercially available analyzers based on the step-gradient principle, and it requires more time than is convenient for many laboratories. Thus, our studies have been directed at modification of the two-column step-gradient procedure for accelerated analysis of hydrolyzates of collagen. The procedure we have devised resolves all of the amino acid components usually present in hydrolyzates of collagen in a period of 215 min.