| Autor: |
Harada, Osamu, Sumita, Suguru, Sugita, Masami, Yamamoto, Tohei |
| Zdroj: |
Bulletin of the Chemical Society of Japan; December 1996, Vol. 69 Issue: 12 p3575-3579, 5p |
| Abstrakt: |
Characterization of pepsin-solubilized type I collagen was examined by a capillary electrophoresis using a capillary coated with α-dodecyl-ω-hydroxy poly(oxyethylene) to reduce protein adsorption and electroosmic flow. A good peak separation for each polypeptide was achieved at pH 5.6—6.5. The peaks were assigned to α1, α2, β11, β12, and γby gel chromatography and reversed phase HPLC. It is found that each αchain signal split into several peaks, reflecting various residues of teropeptide. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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