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Cytochemistry Of Phosphatases Of The Sarcoplasmic Reticulum by Lois W. Tice; A. G. Engel is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The distribution of the Mg-dependent ATPase associated with a microsomal fraction of rabbit psoas muscle was studied histochemically and its localization in relation to the vesicles of the fraction and to the structure of intact fixed muscle was determined. Although enzyme activity was retained after fixation in hydroxyadipaldehyde and in glyoxal, it was lost after fixation in glutaraldehyde or after 4 hr fixation in formaldehyde. Activity was optimally demonstrated when incubations were conducted at 17°C, in media containing 125 mM Trismaleate buffer, pH 7.5, 5 mM ATP, 4 mM MgCl~2~, and 1 mM Pb(NO~3~)~2~. After such incubations, activity was present throughout the sarcoplasmic reticulum, but was absent from the T system. Activation by Na or K could not be demonstrated histochemically. However, the other biochemical properties of the enzyme in the isolated vesicles and in intact muscle were similar with respect to Mg dependence, substrate specificity, inhibition by Ca, N-ethyl maleimide, __p__-hydroxymercuribenzoate, and lack of inhibition by ouabain.

Who reads Cytochemistry Of Phosphatases Of The Sarcoplasmic Reticulum?

Author

Lois W. Tice; A. G. Engel

Publisher

Rockefeller University Press.; The Rockefeller University Press; Rockefeller University Press; ScienceOpen (ISSN 0021-9525)

Published

1966

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)