Ethoxylated alcohol (Neodol-12) and other surfactants in the assay of protein kinase C
Most commonly used surfactants were found to be inhibitors of partially purified rat brain protein kinase C at or above their critical micellar concentrations (CMC). These include sodium lauryl sulfate, deoxycholate, octyl glucoside, dodecyl trimethylammonium bromide, linear alkylbenzene sulfonate a...
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Published in | Biochimica et biophysica acta, Protein structure and molecular enzymology Vol. 992; no. 3; pp. 362 - 368 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
Published |
01.01.1989
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Subjects | |
Online Access | Get full text |
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Summary: | Most commonly used surfactants were found to be inhibitors of partially purified rat brain protein kinase C at or above their critical micellar concentrations (CMC). These include sodium lauryl sulfate, deoxycholate, octyl glucoside, dodecyl trimethylammonium bromide, linear alkylbenzene sulfonate and Triton X-100. Several detergents, including the nonionic surfactants digitonin and Neodol-12 (ethoxylated alcohol), did not inhibit protein kinase C activity, even at concentrations greater than their CMC, while the anionic surfactant, AEOS-12 (ethoxylated alcohol sulfate), inhibited enzyme activity only slightly (less than 8%). The results indicate that activity of protein kinase C can be modified by the conditions of the assay and by the detergents used to extract the enzyme. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 content type line 23 ObjectType-Feature-2 |
ISSN: | 0167-4838 |