Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.6.3.1 (Mg2+-ATPase)
 1,484 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The hydrophobic compound diethylstilbestrol inhibits the generation of the proton gradient and the membrane potential in chromatophores from Rhodospirillum rubum and dissipates proton gradients over asolectin vesicle membranes. The Ca2+-ATPase activity of chromatophores, of purified F0F1-ATPase and of purified F1-ATPase is also decreased in the presence of diethylstilbestrol. Other repressed activities are the pyrophosphatase activity of soluble pyrophosphatase from yeast and the NADH oxidation by L-lactate:NAD oxidoreductase. We have previously reported that also ATP synthesis, PPi synthesis and PPi hydrolysis of R. rubrum chromatophores are inhibited by diethylstilbestrol [Strid et al. (1987) Biochim. Biophys. Acta 892, 236-244]. Addition of bovine serum albumin reverses or prevents diethylstilbestrol-induced inhibition of the activities tested. On the other hand, the Mg2+-ATPase activity of chromatophores, purified F0F1-ATPase and purified F1-ATPase are stimulated by low concentrations of diethylstilbestrol. On the basis of its hydrophobicity and the reversal of its inhibition by bovine serum albumin, diethylstilbestrol is proposed to act unspecifically on membranes and at hydrophobic domains of proteins. Such an attack upon the subunits of the F1-ATPase, altering the subunit interactions, is proposed to explain the different results obtained for the Ca2+-ATPase and the Mg2+-ATPase.
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PMID:Diethylstilbestrol. Interactions with membranes and proteins and the different effects upon Ca2+- and Mg2+-dependent activities of the F1-ATPase from Rhodospirillum rubrum. 290 53

Although there is some evidence that extrachoroidal sites for the production of cerebrospinal fluid (CSF) are important, the choroid plexuses in the ventricles contribute the major part of CSF formation. The exact mechanism for CSF production is not fully understood. In order to study this mechanism from the enzyme histochemical standpoint, the previously reported studies are reviewed, in addition to the authors' own electron microscopic enzyme histochemical observations on this tissue. The ultrastructure and enzyme biochemistry of choroid plexus epithelial cells are considered, together with the histochemistry of the following enzymes: alkaline and acid phosphatase, Mg2+-ATPase, Na+, K+-ATPase, glucose-6-phosphatase, thiamine pyrophosphatase, adenylate cyclase, carbonic anhydrase, oxidoreductase, esterase, several hydrolases, and other enzymes. Finally, CSF formation and active transport in the choroid plexus epithelial cells are discussed, mainly in terms of the results of our enzyme cytochemical observations on Na+, K+-ATPase and carbonic anhydrase in this tissue.
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PMID:The enzyme histochemistry of the choroid plexus. 683 Nov 99