Year: 1950
Type: article
Abstract: PANCREATIC ELASTASE 387 split peptide linkages, but acts in rendering the elastin soluble.It is our belief that possibly the long rod-shaped molecules of elastin are transformed into globular ones without the liberation of amino-acids.Verification of this hypothesis requires further in- vestigation.The occurrence of an elastolytic enzyme in the humranor animal organismhasnot beenshownbefore.Eijkman (1904) studied the elastin-dissolving activity of bacteria.He prepared, from the lungs of calves, from ligamenta nuchae and from arteries, culture media with which he demonstrated the lysis of elastin as the result of bacterial action.Bacillus pyocyaneuqs showed the highest activity.SUMMARY 1. Pancreatic extract contains an enzyme which dissolves the elastic fibres of the aorta wall and which is called elastolytic enzyme or elastase. Trypsin prepared according to Kunitz & Northrop (1935-6) has little effect on arteries.3. The elastase dissolves only the elastin in the aorta wall and leaves the collagen unchanged.4. Elastase does not liberate amino-acids from the aorta wall, but insoluble elastin is changed into a soluble protein.5. The pH optimum of the elastase (10.3) is more alkaline than that of trypsin.
Source: Biochemical Journal
DOI: 10.1042/bj0460387
Author: B. Chance
Institution: University of Cambridge
Language: English
Subfield: Cancer Research
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W2271627760