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At least 451 records · Page 25Linked to original sources
PubMed1976

The further heterogeneity of creatine kinase. Presence of isoenzymes of cathodic mobility in rat tissues.

Supernatant fractions from rat tissue homogenates were examined for creatine kinase (EC 2.7.3.2) isoenzymes by agarose gel electrophoresis at pH 8.6. The distribution of the various isoenzymes, and their relative contributions to the total tissue creatine kinase, is stated. A previously unreported isoenzyme associated with brain and kidney preparations is described. It is a minor contributor to brain creatine-kinase activity but is the major isoenzyme for kidney. The presence of an additional isoenzyme for cardiac tissue was confirmed; this isoenzyme exhibits similar levels of activity to that of the MB isoenzyme.

Animals↗
PubMed1987

The mechanism of cathode reduction of oxygen in a carbon carrier-laccase system.

The influence of temperature, oxygen pressure and inhibitors of laccase on the dioxygen electroreduction reaction has been examined at different solution pH. On the basis of obtained data, a reaction mechanism including electron transfer from the enzyme active site to the oxygen molecule is suggested as the slow step.

Electrochemistry↗
PubMed2004

A performance comparison of choline biosensors: anodic or cathodic detections of H2O2 generated by enzyme immobilized on a conducting polymer.

Amperometric choline biosensors were fabricated by the covalent immobilization of an enzyme of choline oxidase (ChO) and a bi-enzyme of ChO/horseradish peroxidase (ChO/HRP) onto poly-5,2':5',2"-terthiophene-3'-carboxylic acid (poly-TTCA) modified electrodes (CPMEs). A sensor modified with ChO utilized the oxidation process of enzymatically generated H(2)O(2) in a choline solution at +0.6V. The other one modified with ChO/HRP utilized the reduction process of H(2)O(2) in a choline solution at -0.2V. Experimental parameters affecting the sensitivity of sensors, such as pH, applied potential, and temperature were optimized. A performance comparison of two sensors showed that one based on ChO/HRP/CPME had a linear range from 1.0 x 10(-6) to 8.0 x 10(-5) M and the other based on ChO/CPME from 1.0 x 10(-6) to 5.0 x 10(-5) M. The detection limits for choline employing ChO/HRP/CPME and ChO/CPME were determined to be about 1.0 x 10(-7) and 4.0 x 10(-7) M, respectively. The response time of sensors was less than 5s. Sensors showed good selectivity to interfering species. The long-term storage stability of the sensor based on ChO/HRP/CPME was longer than that based on ChO/CPME.

Alcohol Oxidoreductases↗