| Autor: |
Rubinstein, M, Rubinstein, S, Familletti, P C, Miller, R S, Waldman, A A, Pestka, S |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; February 1979, Vol. 76 Issue: 2 p640-644, 5p |
| Abstrakt: |
A method of fractionating proteins by high-performance liquid partition chromatography has been developed and used for isolation and purification to homogeneity of one of the species of human leukocyte interferon. The homogeneous interferon exhibited a sharp peak on high-performance liquid chromatography and a single narrow band on sodium dodecyl sulfate/polyacrylamide gel electrophoresis in the presence of 2-mercaptoethanol. Extraction of the gel gave a single sharp peak of antiviral activity coinciding with the protein band. The specific activity of pure interferon was found to be 2--4 X 10(8) units/mg, based on amino acid analysis. The molecular weight is 17,500--18,000. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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