| Autor: |
Reed, S I, Hadwiger, J A, Lörincz, A T |
| Zdroj: |
Proceedings of the National Academy of Sciences of the United States of America; June 1985, Vol. 82 Issue: 12 p4055-4059, 5p |
| Abstrakt: |
Antibodies raised against the protein encoded by a lacZ-CDC28 in-frame fusion were shown to immunoprecipitate the CDC28 product from yeast cell lysates. The polypeptide p36CDC28 is a phosphoprotein of apparent Mr 36,000. Immune complexes prepared from yeast cell lysates by using anti-CDC28 antibody were found to possess a protein kinase activity, as determined by the transfer of label from [gamma-32P]ATP to a coprecipitated Mr 40,000 protein of unknown identity or function (p40). This activity was absent or thermolabile when extracts were prepared from several different cdc28 temperature-sensitive strains. The protein kinase activity was dependent on Zn2+ and transferred phosphate specifically to serine and threonine residues. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
