The influence of cadmium ions on the adsorption of prothrombin onto Al(OH)3 as a means to purify prothrombin
| Autor: | P.P. Devilee, H.C. Hemker, B.M. Bas |
|---|---|
| Přispěvatelé: | Biochemie |
| Rok vydání: | 1975 |
| Předmět: |
chemistry.chemical_classification
Cadmium Chromatography chemistry.chemical_element Biochemistry Genetics and Molecular Biology (miscellaneous) Ion Amino acid Thrombin Adsorption Column chromatography Coagulation chemistry Yield (chemistry) medicine circulatory and respiratory physiology medicine.drug |
| Zdroj: | Biochimica et Biophysica Acta (BBA)-Protein Structure, 379(1), 172-179. Elsevier BV |
| ISSN: | 0005-2795 |
| DOI: | 10.1016/0005-2795(75)90019-7 |
| Popis: | 1. 1.|In the presence of CdSO4 (1 mM), Al(OH)3 (1.3% w/v) completely adsorbs the coagulation factors VII, IX, and X from normal plasma, but factor II (prothrombin) is adsorbed for about 50% only. 2. 2.|A purification procedure for factor II is developed, using Al(OH)3 adsorption in the presence of Cd2+ as a first step and using column chromatography only once. A 750-fold purification is obtained at a 24% yield. 3. 3.|Comparison of the prothrombin thus obtained, with prothrombin isolated by the method of Kisiel and Hanahan (Biochim. Biophys. Acta (1973) 304, 103–113) does not show significant differences in amino acid composition, N-terminal amino acid, molecular weight or immunological properties. 4. 4.|Comparison of the two prothrombin preparations in a thrombin-generating system shows that although the final yield of thrombin from a given amount of prothrombin in both preparations is the same, the initial velocity of thrombin formation from our preparation is comparable to that of native prothrombin, whereas the other preparation is converted significantly slower. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|