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Journal archive > 2007 > N 1 January-February

IDENTIFICATION OF Ca2+-ACTIVATED Mg2+-DEPENDENT
АТP-HYDROLASE ACTIVITY OF MEMBRANE MICROSOMAL FRACTION
OF LOACH EMBRYO (Misgurnus fossilis L.)

M. V. Tselevych, R. V. Fafula, M. B. Galan, D. I. Sanagurski

Ivan Franko Lviv National University, Ukraine;

The functional confirmation of availability of Са2+ transport initially-active systems in the embryo cells of loach Misgurnus fossilis L. has been obtained. Using thapsigargin, the specific inhibitor of endoplasmic reticulum of Са2+, Mg2+-АТРase, this enzyme activity was divided into thapsigargin-sensitive (actually endoplasmic reticulum Са2+, Mg2+-АТРase) and thapsigargin-insensitive (plasma membrane Ca2+, Mg2+-ATPase) constituents. The Ca2+-independent Mg2+-dependent ATPase activity makes above 39.7% of the common Са2+, Mg2+-ATPase activity of embryo loach. The periodic changes of Са2+, Mg2+-АТРase activity (except for the changes of plasma membrane Ca2+, Mg2+-ATPase activity) were found out, which coincide with periodic [Ca2+]і oscillations during the synchronous divisions of loach blastomers embryos.

Key words: loach embryos, Ca2+-activated Mg2+-dependent ATPase, Mg2+-dependent ATPase, plasma membrane, endoplasmic reticulum, blastomers divisions.

The original article in Ukrainian is available for download in PDF format.

© The Ukrainian Biochemical Journal