[Casein kinase type II during lens fiber differentiation in amphibians].
cAMP-independent protein kinase activity of casein type was found in Rana temporaria eye lens. The highest activity was observed in "cortex" lens fibres, and decreased two-fold in lens epithelium. Minimum activity was found in lens "nucleus" fibres. Thus, protein kinase activity is characteristic of metabolically active differentiating lens cells. Enzyme fraction showed almost complete binding to the immobilized RNA. The enzyme was inhibited by heparine, phosphorylated casein (but not histones). It could use either ATP or GTP as a source of phosphate, and caused modification of serine and threonine residues in casein molecule. The protein kinase from lens epithelium and cortex was purified 6,000-7,000-fold and was identified as a type II casein kinase.
Elizarov
S M
SM
Simirskiĭ
V N
VN
D000663:Amphibians / Q000378:metabolism*; D000818:Animals; D001345:Autoradiography; D047388:Casein Kinases; D002454:Cell Differentiation / Q000502:physiology; D002850:Chromatography, Gel; D002853:Chromatography, Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D007908:Lens, Crystalline / Q000166:cytology / Q000201:enzymology*; D011494:Protein Kinases / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D011896:Rana temporaria
D011494:Protein Kinases; D047388:Casein Kinases
Kazeinovaia kinaza tipa II v protsesse differentsirovki volokon khrustalika amfibii.