| Autor: |
Slinchenko NM; Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv. kinet@biochem.kiev.ua |
| Jazyk: |
ukrajinština |
| Zdroj: |
Ukrains'kyi biokhimichnyi zhurnal (1999 ) [Ukr Biokhim Zh (1999)] 2000 Nov-Dec; Vol. 72 (6), pp. 35-8. |
| Abstrakt: |
Myometrium cell plasma membrane Ca2+, Mg(2+)-ATPase purified by an affinity chromatography on calmodulin-sepharose 4B is calmodulin-dependent enzyme. Concentration of calmodulin required for half-maximal activation of enzyme was about 26 nM. By unlike to the enzymes originated from other tissues sensitivity to the calmodulin of the myometrial sarcolemma Ca(2+)-transporting ATPase was lower: calmodulin increased Vmax of ATPase about 1.25-fold, the apparent constant of the activation of enzyme by Ca2+ failed to alter independently on the phospholipid presenting at the enzyme isolation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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