By means of NED-affinity column chromatography, two distinct protein kinases have been selectively purified from the crude membrane extract of mouse brain. One (designated P-I kinase) was eluted from the column by the buffer containing 5 mM EGTA and the other (designated P-II kinase) was eluted by the buffer containing 0.6 M KCl. The activity of A-kinase was detected in the column passed through fraction. Biochemical characteristics of P-I and P-II kinases corresponded exactly to those of C-kinase and casein kinase II (CK-II), respectively. In addition, immunoprecipitate experiment using anti-CK-II antiserum against the beta-subunit of Drosophila CK-II showed that P-II kinase is identical to CK-II and the 62 kDa cellular polypeptide is associated with the kinase.
|Number of pages||11|
|Journal||The Kitasato archives of experimental medicine|
|Publication status||Published - 1992 Apr|
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