The purification and characterization of bovine salivary proteins by electrophoretic procedures
โ Scribed by Robert D. McLaren; James T. McIntosh; Gregory W. Howe
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 738 KB
- Volume
- 8
- Category
- Article
- ISSN
- 0173-0835
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๐ SIMILAR VOLUMES
A lipid transfer protein was isolated from bovine liver. Following the release of soluble proteins from liver microsomes, the transfer protein was purified 75-fold to near homogeneity by a combination of DEAE-celiulose ion exchange, Sephadex G-200 gel permeation, and hydroxylapatite chromatography.
We have explored various chromatographic procedures with the intention of establishing an isolation procedure that would allow us to isolate a large quantity of PSA-ACT (prostate specific antigen-a, -antichymotrypsin) complex either from patients' sera or from incubation mixtures of free PSA and pro