The application of collagenase, purified by affintiy chromatography, to the isolation of insoluble elastin from bovine aorta
| Autor: | A. Serafini-Fracassini, J.M. Field, Michele Spina, G. Garbin |
|---|---|
| Rok vydání: | 1975 |
| Předmět: |
Clostridium histolyticum Collagenase
Biochemistry Genetics and Molecular Biology (miscellaneous) Guanidines Chromatography Affinity Hydrolysis Affinity chromatography medicine.ligament medicine Animals Amino Acid Sequence Amino Acids Aorta Bovine aorta chemistry.chemical_classification Chromatography Binding Sites biology Chemistry Hexosamines Chromatography Ion Exchange Amino acid Elastin Microbial Collagenase Biochemistry cardiovascular system Collagenase Ligamentum nuchae biology.protein Cattle medicine.drug Protein Binding |
| Zdroj: | Biochimica et biophysica acta. 400(1) |
| ISSN: | 0006-3002 |
| Popis: | Clostridium histolyticum collagenase (clostridiopeptidase A, EC 3.4.4.19), purified by affinity chromatography, was applied to the isolation of insoluble elastin from bovine aorta. The extremely low level of N-terminal residues (1.6 mol per 10 6 g of protein) present in this preparation indicated the almost complete lack of hydrolytic damage caused by the isolation procedure. The amino acid profile of the aortic elastin was found to be almost identical to that of insoluble elastin prepared from bovine ligamentum nuchae by the same method. |
| Databáze: | OpenAIRE |
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