﻿<?xml version="1.0" encoding="utf-8"?><rss version="2.0"><channel><title>Enzyme Research</title><link>http://www.sage-hindawi.com</link><description>The latest articles from SAGE-Hindawi Access to Research</description><copyright>&amp;#169; 2010, SAGE-Hindawi Access to Research. All rights reserved.</copyright><item><title>Hyperbaric Oxygen Exposure Reduces Age-Related Decrease in Oxidative Capacity of the Tibialis Anterior Muscle in Mice</title><link>http://www.sage-hindawi.com/journals/er/2010/824763.html</link><description>The effects of exposure to hyperbaric oxygen on the oxidative capacity of the skeletal muscles in mice at different ages were investigated. We exposed 5-, 34-, 55-, and 88-week-old mice to 36&amp;#37; oxygen at 950&amp;#x2009;mmHg for 6 hours per day for 2 weeks. The activities of succinate dehydrogenase (SDH), which is a mitochondrial marker enzyme, of the tibialis anterior muscle in hyperbaric mice were compared with those in age-matched mice under normobaric conditions (21&amp;#37; oxygen at 760&amp;#x2009;mmHg). Furthermore, the SDH activities of type IIA and type IIB fibers in the muscle were determined using quantitative histochemical analysis. The SDH activity of the muscle in normobaric mice decreased with age. Similar results were observed in both type IIA and type IIB fibers in the muscle. The decrease in the SDH activity of the muscle was reduced in hyperbaric mice at 57 and 90 weeks. The decreased SDH activities of type IIA and type IIB fibers were reduced in hyperbaric mice at 90 weeks and at 57 and 90 weeks, respectively. We conclude that exposure to hyperbaric oxygen used in this study reduces the age-related decrease in the oxidative capacity of skeletal muscles.</description><Author>Takahiro Nishizaka, Fumiko Nagatomo, Hidemi Fujino, Tomoko Nomura, Tomohiko Sano, Kazuhiko Higuchi, Isao Takeda, and Akihiko Ishihara</Author><copyright>&amp;#169; 2010, SAGE-Hindawi Access to Research. All rights reserved.</copyright></item><item><title>Enzyme Inhibition by Molluscicidal Components of Myristica fragrans Houtt. in the Nervous Tissue of Snail Lymnaea acuminata</title><link>http://www.sage-hindawi.com/journals/er/2010/478746.html</link><description>This study was designed to investigate the effects of molluscicidal components of Myristica fragrans Houtt. (Myristicaceae) on certain enzymes in the nervous tissue of freshwater snail Lymnaea acuminata Lamarck (Lymnaeidae). In vivo and in vitro treatments of trimyristin and myristicin (active molluscicidal components of Myristica fragrans Houtt.) significantly inhibited the acetylcholinesterase (AChE), acid and alkaline phosphatase (ACP/ALP) activities in the nervous tissue of Lymnaea acuminata. The inhibition kinetics of these enzymes indicates that both the trimyristin and myristicin caused competitive noncompetitive inhibition of AChE. Trimyristin caused uncompetitive and competitive/noncompetitive inhibitions of ACP and ALP, respectively whereas the myristicin caused competitive and uncompetitive inhibition of ACP and ALP, respectively. Thus results from the present study suggest that inhibition of AChE, ACP, and ALP by trimyristin and myristicin in the snail Lymnaea acuminata may be the cause of the molluscicidal activity of Myristica fragrans.</description><Author>Preetee Jaiswal, Pradeep Kumar, V. K. Singh, and D. K. Singh</Author><copyright>&amp;#169; 2010, SAGE-Hindawi Access to Research. All rights reserved.</copyright></item><item><title>Purification, Characterization, and Effect of Thiol Compounds on Activity of the Erwinia carotovora L-Asparaginase</title><link>http://www.sage-hindawi.com/journals/er/2010/165878.html</link><description>L-asparaginase was extracted from Erwinia carotovora and purified by ammonium sulfate fractionation (60&amp;#8211;70&amp;#37;), Sephadex G-100, CM cellulose, and DEAE sephadex chromatography. The apparent Mr of enzyme under nondenaturing and denaturing conditions was 150&amp;#x2009;kDa and 37&amp;#x00B1;0.5&amp;#x2009;kDa, respectively. L-asparaginase activity was studied in presence of thiols, namely, L-cystine (Cys), L-methionine (Met), N-acetyl cysteine (NAC), and reduced glutathione (GSH). Kinetic parameters in presence of thiols (10&amp;#x2013;400 &amp;#x03BC;M) showed an increase in Vmax values (2000, 2223, 2380, 2500, and control 1666.7&amp;#x2009;&amp;#x03BC;moles mg-1min-1) and a decrease in Km values (0.086, 0.076, 0.062, 0.055 and control 0.098&amp;#x2009;mM) indicating nonessential mode of activation. KA values displayed propensity to bind thiols. A decrease in Vmax/Km ratio in concentration plots showed inverse relationship between free thiol groups (NAC and GSH) and bound thiol group (Cys and Met). Enzyme activity was enhanced in presence of thiol protecting reagents like dithiothreitol (DTT), 2-mercaptoethanol (2-ME), and GSH, but inhibited by p-chloromercurybenzoate (PCMB) and iodoacetamide (IA).</description><Author>Suchita C. Warangkar and Chandrahas N. Khobragade</Author><copyright>&amp;#169; 2010, SAGE-Hindawi Access to Research. All rights reserved.</copyright></item></channel></rss>