Abstract
A simple procedure was devised for isolating from homogenates of mitotic cells the human homolog to the fission yeast cdc2 gene product. The identity of the purified protein was established with anti-p34 cdc2 antibodies and p13 suc1 , both specific ligands for p34 cdc2 . Active-site labeling with oxidized [α 32P]ATP showed the purified molecule to be an ATP-binding protein. Its ability to phosphorylate casein but not histone, and its phosphorylation on tyrosine, detected by anti-phosphotyrosine antibodies, indicates the form of p34 cdc2 purified is the inactive or apoenzyme form. Purified quantities of human p34 cdc2 should be of considerable value in establishing the mechanism of its activation at mitosis by phosphatases.
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