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The reactions of catalase in the presence of the notatin system
Open accessAbstract
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.
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Cited by
Gaetani, G., Galiano, S., Canepa, L., Ferraris, A., & Kirkman, H. (1989) · Blood · doi:10.1182/blood.v73.1.334.334 · Cited by 298
Reactions of Bovine Liver Catalase with Superoxide Radicals and Hydrogen Peroxide
Lardinois, O. M. (1995) · Free Radical Research · doi:10.3109/10715769509147544 · Cited by 91
Metadata
- Authors
- Chance, B.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 1950-04-01
- Volume
- 46
- Issue
- 4
- Pages
- 387-402
- ISSN
- 0306-3283 (ISSN-L)
- OpenAlex
- W2271627760
- Cited by
- 175
- References
- 0
- FWCI
- 7.03
- Type
- journal article
- Language
- en
- Open access
- bronze
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