Ospina B, Fernández-Renart M
Instituto de Investigaciones Biomédicas del C.S.I.C., Madrid, Spain.
Biochim Biophys Acta. 1990 May 22;1052(3):483-8. doi: 10.1016/0167-4889(90)90159-b.
Three different casein kinases type I have been characterized and partially purified from vegetative cells of Dictyostelium discoideum. The enzymes have been classified as type I because they are excluded from DEAE cellulose columns and do not utilize GTP as phosphoryl donor. We have named these activities as casein kinases IA, IB and IC respectively, according to the elution profile on phosphocellulose chromatography. The three activities differ in: the sensitivity to heparin inhibition; the salt optimum for activity and the amino acids phosphorylated, using casein as substrate. Experiments carried out in conditions that favor autophosphorylation indicate that casein kinase IB could have a 53 kDa subunit, susceptible to autophosphorylation in vitro.
