title: [Several properties of calmodulin from the myometrium of female rabbits].
abstract: Calmodulin, a Ca2+-binding protein activator of a series of enzymes, was isolated from the female rabbit myometrium in a homogenous state by DEAE-cellulose chromatography. Purification of calmodulin produced a 120-fold increase in its specific activity with the quantitative yield accounting for as high as 10%. Isoelectrical focusing on polyacrylamide gel plates revealed that the activator pI is 5.45 at the state of functional rest and 5.17--at pregnancy. The molecular mass determined by electrophoresis in DS-polyacrylamide gel is 18.000, that determined by the Sephadex G-200 column gel-filtration--21 000. The content of calmodulin in the myometrium at functional rest is 3 mg, at pregnancy--10 mg per 100 g of tissue; Kbound--0.25 X 10(8)M-1 and 0.12 X 10(8)M1, respectively.
mesh_terms: D000818:Animals; D002147:Calmodulin / Q000302:isolation & purification / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D007700:Kinetics; D008970:Molecular Weight; D009215:Myometrium / Q000378:metabolism*; D011247:Pregnancy; D011817:Rabbits
chemical_list: D002147:Calmodulin
vernacular_title: Nekotorye svoĭstva kal'modulina miometriia krol'chikh.