PROTEIN-KINASE-C AND CASEIN-KINASE-2 PHOSPHORYLATE IN-VITRO PROTEINS OF THE ANNEXIN FAMILY FROM EGGS OF LOACH MISGURNUS-FOSSILIS

A mixture of proteins of the annexin family was obtained from the cyto plasm of mature eggs of leach Misgurnus fossilis (by reprecipitation w ith acid phospholipids in the presence of Ca2+). This mixture comprise d five proteins with molecular weights of 58, 38, 36, 35, and 31 kD. P olyclonal rabbit antibodies against the major 31-kD protein were obtai ned. Western blot analysis showed that the obtained antibodies exhibit a high specificity towards the 31-kD protein from eggs and other tiss ues of leach and zebrafish (Brachydanio rerio). The analysis of cDNA c orresponding to the 31-kD protein by screening the zebrafish cDNA libr ary confirmed that this protein belongs to the annexin family. Phospho rylation of the obtained annexins in vitro was studied. It is shown th at the 58-kD protein is phosphorylated by casein kinase 2 (CK2), where as the 38-, 36-, 35-, and 31-kD proteins are phosphorylated by protein kinase C (PKC).