Alwasel, Rosmarinic acid inhibits some metabolic enzymes including glutathione S-transferase, lactoperoxidase, acetylcholinesterase, butyrylcholinesterase and carbonic
anhydrase isoenzymes, J.
There are a number of examples: in carbonic
anhydrase, Zn works in a coordinated way with the C[O.sub.2] substrate; in carboxipeptidase, it takes an active role in the breakage of the peptide union; in multisub union enzymes such as aspartate transcarbamylate, Zn plays a structural role by coordinating the positions of the regulator and catalytic subunits; in another structural role, the Cu, Zn-superoxide-dismutase requires Zn to position the Cu atom in the channel accessed by the substrate; in Zn finger proteins, the [Zn.sup.2+] helps to stabilize the structure of curls, which contact the major and minor grooves of the DNA (Auld, 2009).
Inversely, osmotic and carbonic
anhydrase inhibitors lead to a significant decrease of lithium levels.
Comparisons of other characteristics demonstrated that the use of [beta]-blocker or carbonic
anhydrase inhibitor eyedrops was more common in the visual field progression group.
Rafajova et al., "Hypoxia activates the capacity of tumor-associated carbonic
anhydrase IX to acidify extracellular pH," FEBS Letters, vol.
Socorro et al., "The structure of carbonic
anhydrase IX is adapted for low-pH catalysis," Biochemistry, vol.
Carbonic
anhydrase IX (CAIX) is a transmembrane protein that catalyzes the hydration of carbon dioxide to carbonic acid, modulating pH [20].
Capsaicin: A potent inhibitor of carbonic
anhydrase isoenzymes.
Dorzolamide is a carbonic
anhydrase inhibitor (CAI) that reduces the activity of carbonic
anhydrase II secreted by non-pigmented ciliary epithelial cells, which keeps bicarbonate ions from being transported along with the sodium cation to the posterior chamber of the eye.
(12) Another possible mechanism is the presence of high titers of an autoantibody directed against carbonic
anhydrase II.
The obtained pellet containing intact cells was resuspended with 20 mM Tris-sulfate buffer, pH 8.3, and the extracellular carbonic
anhydrase enzyme activity were immediately measured using the titrimetric method of Wilbur and Anderson with modification according to Rigobello-Masini et al.
These differences result from larger increases in expression of the drivers behind ion transport ([Na.sup.+]/[K.sup.+]-ATPase, cytoplasmic carbonic
anhydrase) in green phase and female crabs.
