Structure and activity of factor D̄ of the alternative pathway of human complement
<p>1. A method for the purification of the serine protease,factor D,was developed using conventional chromatographic procedures. The final product was homogeneous as judged by SDS/polyacrylamide gel electrophoresis, its migration as a single component in ion exchange and gel filtration media,...
| Päätekijät: | , |
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| Muut tekijät: | |
| Aineistotyyppi: | Opinnäyte |
| Kieli: | English |
| Julkaistu: |
1981
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| Aiheet: |