Abstract
A simple method for the isolation of α-chains of different collagen types was developed. The procedure involves sodium dodecyl sulfatae-polyacrylamide gel electrophoresis followed by electroelution of separated and defixed collagen α-chains. Collagen types I, II, III and V from different porcine tissues were recovered in high quantity (>95%) and purity (>98%) as evidenced by amino acid analysis. The procedure can be used for sample quantities smaller than required for conventional methods, e.g, chromatographic procedures.
| Original language | English |
|---|---|
| Journal | Journal of Chromatography A |
| Volume | 758 |
| Issue number | 2 |
| Pages (from-to) | 313-318 |
| Number of pages | 6 |
| ISSN | 0021-9673 |
| DOIs | |
| Publication status | Published - 17.01.1997 |
Funding
This work was supportedb y DFG (Deutsche For-schungsgemeinschaSftF;B 367-A1 and Br 1146/2-1), by a grant from the BMFT (Bundesministerium ftir Forschung und Technologie0, 1 KM 9303) and by a grant from the registereds ociety for investigation and fight of rheumatoid diseases (Bad BramstedtG, ermany).
Research Areas and Centers
- Academic Focus: Center for Infection and Inflammation Research (ZIEL)