| Autor: |
D, Filippi-Foveau, M, Sciaky, N, Limozin, C, Dalmasso, G, Laurent-Tabusse |
| Jazyk: |
francouzština |
| Rok vydání: |
1976 |
| Předmět: |
|
| Zdroj: |
Biochimie. 58(9) |
| ISSN: |
0300-9084 |
| Popis: |
Bovine erythrocyte carbonic anhydrase CI consists of 259 amino acid residues including 18 lysines and 9 arginines. Its primary structure has been first investigated by isolation and sequence determination of the tryptic units. Acidification of the tryptic hydrolysate leads to the precipitation of 40% of the peptidic material. All the acid soluble peptides were isolated from the supernatant by chromatography on Dowex 50 W-X2 and Dowex 1-X2 followed by purification of heterogeneous fractions. Two of the three acid insoluble peptides were obtained in a pure form from the whole tryptic hydrolysate by gel filtration on Sephadex G-50 and chromatography on DEAE-Sephadex in alkaline medium. The sequence of the so isolated tryptic units has been determined with the exception of two of them obtained in a very poor yield. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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