作者: Cesar H. Casale , Alejandra del C. Alonso , Héctor S. Barra
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摘要: Membranes from brain tissue contain tubulin that can be isolated as a hydrophobic compound by partitioning into Triton X-114. The behavior of this is due to the formation complex with α-subunit Na+,K+-ATPase. In present work we show interaction Na+K+-ATPase inhibits enzyme activity. We found magnitude inhibition correlated with: (1) concentration acetylated isoform in preparation used, and (2) amount compound. addition, some compounds involved catalytic action were assayed determine their effects on inhibitory capability enzyme. effect was only slightly decreased ATP at relatively low nucleotide (0.06 mM). NaCl (1-160 mM) KCl (0.2-10 showed no whereas inorganic phosphate abolished concentration-dependent manner.