A simple two-step procedure for obtaining highly purifed human tibrinopeptides is described. This technique utilizes batch adsorption to a Clll silica-coated matrix packed in a disposable cartridge. This step serves both to concentrate and desalt fibrinopeptides released into the supernatant during
Purification of adenovirus hexon protein by high-performance liquid chromatography
β Scribed by Matti Waris; Pekka Halonen
- Publisher
- Elsevier Science
- Year
- 1987
- Tongue
- English
- Weight
- 459 KB
- Volume
- 397
- Category
- Article
- ISSN
- 1873-3778
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β¦ Synopsis
Adenovirus (Type 2)-infected HeLa cells were sonicated and treated with 1,1,2-trichlorotrifluoroethane. The water-soluble extract was ultracentrifuged and the supernatant, containing the dissociated proteins, was subjected to anion-exchange high-performance liquid chromatography on a Mono Q column in 50 mM bis-Tris-HCl (pH 6.5). Elution with a linear salt gradient resulted in a major peak, containing the hexon protein.
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A new procedure using high-performance liquid chromatography for the rapid separation of cellulase proteins is described. The cellulase components of Trichoderma reesei are fractionated on a DEAE anion-exchange column using a phosphate buffer at pH 6.2. Activities of the individual components obtain