Effects of metabolic syndrome on masseter muscle of male Wistar rats.

The aim of this study was to investigate the association between metabolic syndrome (MetS) and the metabolic indicators of masticatory muscles in an animal model. A total of 16 male Wistar rats were used. To induce MetS, 10 rats were fed with standard rat chow and 32% sucrose solution ad libitum for 16 wk.

Preparative-scale kinetic resolution of racemic styrene oxide by immobilized epoxide hydrolase.

Epoxide hydrolase from Aspergillus niger was immobilized onto the modified Eupergit C 250 L through a Schiff base formation. Eupergit C 250 L was treated with ethylenediamine to introduce primary amine groups which were subsequently activated with glutaraldehyde. The amount of introduced primary amine groups was 220 μmol/g of the support after ethylenediamine treatment, and 90% of these groups were activated with glutaraldehyde.

Covalent immobilization of catalase onto spacer-arm attached modified florisil: characterization and application to batch and plug-flow type reactor systems.

Catalase was covalently immobilized onto florisil via glutaraldehyde (GA) and glutaraldehyde+6-amino hexanoic acid (6-AHA) (as a spacer arm). Immobilizations of catalase onto modified supports were optimized to improve the efficiency of the overall immobilization procedures. The V(max) values of catalase immobilized via glutaraldehyde (CIG) and catalase immobilized via glutaraldehyde+6-amino hexanoic acid (CIG-6-AHA) were about 0.

Kinetic properties and storage stability of catalase immobilized on to florisil.

The covalent immobilization of bovine liver catalase (CAT) on to florisil via glutaraldehyde was investigated. Optimum immobilization pH and temperature were determined as pH 6.0, 10 degrees C respectively, while the amount of initial CAT per g of carrier and immobilization time was determined as 5 mg g(-1) and 120 min, respectively.

Response of catalase activity to Ag+, Cd2+, Cr6+, Cu2+ and Zn2+ in five tissues of freshwater fish Oreochromis niloticus.

Catalase (CAT, EC 1.11.1.