Corrigendum: Inhibitory Effect of Codeine on Sucrase Activity.

A typographical error appeared in the author's name of the article entitled "Inhibitory Effect of Codeine on Sucrase Activity" by Dariush Minai-Tehrani, Saeed Minoui, Marzie Sepehre, Zohre Sharif-Khodai, Tooka Aavani, Drug Metabolism Letters, 2009; 3(1): 58-60. [1]. Details of the error and a correction are provided here. The fourth author's name in this article was misspelled. Hence it should be read as "Zohreh Sharifkhodaei" as per the request of the author. We regret the error and apologize to readers. The original article can be found online at: https://www.eurekaselect.com/93132/article Original: Zohre Sharif-Khodai Corrected: Zohreh Sharifkhodaei.

Ranitidine induces inhibition and structural changes in sucrase.

Ranitidine is an antagonist of histamine-2 (H(2)) receptor. It is employed to treat peptic ulcer and other conditions in which gastric acidity must be reduced. Sucrase is a hydrolytic enzyme that catalyzes the breakdown of sucrose to its monomer content. A liquid of yeast sucrase was developed for treatment of congenital sucrase-isomaltase deficiency (CSID) in human. In this study, the effect of ranitidine on yeast sucrase activity was investigated. Our results showed that ranitidine binds to sucrase and inhibits the enzyme in a noncompetitive manner. The K(i) and IC(50) values were measured to be about 2.3 and 2.2 mM, respectively. Fluorescence measurement showed conformational changes after binding of ranitidine to the enzyme. The fluorescence spectra showed that ranitidine could bind to both free enzyme and enzyme-substrate complex, which was accompanied with reduction of emission intensity and red shift production.

Inhibition of renal alkaline phosphatase by cimetidine.

Alkaline phosphatase (ALP) belongs to hydrolase group of enzymes. It is responsible for removing phosphate groups from many types of molecules, including nucleotides and proteins. Cimetidine (trade name Tagamet) is an antagonist of histamine H2-receptor that inhibits the production of gastric acid. Cimetidine is used for the treatment of gastrointestinal diseases. In this study the inhibitory effect of cimetidine on mouse renal ALP activity was investigated. Our results showed that cimetidine can inhibit ALP by uncompetitive inhibition. In the absence of inhibitor the V(max) and K(m) of the enzyme were found to be 13.7 mmol/mg prot.min and 0.25 mM, respectively. Both the Vmax and Km of the enzyme decreased with increasing cimetidine concentrations (0- 1.2 mM). The Ki and IC(50) of cimetidine were determined to be about 0.5 mM and 0.52 mM, respectively.

Structural changes and inhibition of sucrase after binding of scopolamine.

Scopolamine (hyoscine) is commonly used as an anticholinergic drug to relieve nausea, vomiting and dizziness of a motion sickness as well as recovery from anesthesia and surgery. Sucrase as a hydrolytic enzyme breaks down sucrose into its monomers, glucose and fructose. The aim of this study was to evaluate the effect of scopolamine on the activity and the structural changes of yeast sucrase. The results showed that binding of scopolamine to sucrase could inhibit the enzyme activity. A non-competitive inhibition was observed in different concentrations of scopolamine (0.6 to 3.6mM). The study by circular dichroism measurement in far-UV showed that the absolute enzyme exhibited a flat negative trough, indicating the presence of alpha-helices and beta-sheet structures in the enzyme. Binding of the inhibitor on the enzyme made a deeper trough at 218nm, suggesting the increasing of beta-sheet content of the enzyme. Fluorescence measurement showed that binding of scopolamine to free enzyme and enzyme-substrate complex increased the peak intensity at 350nm and also induced red shift. Our findings suggest that scopolamine binds to the location other than the active site of enzyme and that the binding causes structural changes and inhibits the enzyme activity.

Inhibitory Effect of Codeine on Sucrase Activity

Codeine is a common drug widely used in some countries as a pain reliever. The effect of codeine on yeast sucrase activity was studied in this report. Non-competitive inhibition was observed using double reciprocal plot. The K(m) of enzyme did not change in the presence of different concentrations of codeine (0.5- 1.5 mM) and was determined about 11.5 mM. The V(max) of enzyme was determined about 8.8 mM/min, and the V(max) decreased in the presence of codeine. The K(i) of codeine was measured by using the reaction rate and the initial concentration of the inhibitor according to the Dixon plot. The K(i) was found to be 0.42 mM and the IC(50) of codeine was determined about 0.875 mM.

Effect of salinity on biodegradation of polycyclic aromatic hydrocarbons (PAHs) of heavy crude oil in soil.

The spillage of crude oil in the soil damages the environment. Polycyclic aromatic hydrocarbons (PAHs) are one of the crude oil components that may be harmful for living organisms. PAHs can disappear from the environment by volatilization and biodegradation. The effect of different NaCl concentrations (0%-5%) on PAHs reduction from the heavy crude oil-contaminated soil was studied. Our results showed that increasing NaCl concentration in soil had decreasing effect on total crude oil and PAHs reduction. The biodegradation of total crude oil was higher in 0% NaCl (41%) while higher total PAHs reduction was observed in 1% NaCl (35%). The lower total crude oil and PAHs reduction were observed in 5% NaCl (12% and 8% respectively). Phenanthrene, anthracene and pyrene reduction were higher in 1% NaCl, while fluoranthene and chrysene reduction were higher in 0% NaCl.