<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Simonian, M A</style></author><author><style face="normal" font="default" size="100%">Nalbandian, R M</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">[Acid and alkaline denaturation of superoxide dismutase].</style></title><secondary-title><style face="normal" font="default" size="100%">Biofizika</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Biofizika</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cattle</style></keyword><keyword><style  face="normal" font="default" size="100%">Erythrocytes</style></keyword><keyword><style  face="normal" font="default" size="100%">Hydrogen-Ion Concentration</style></keyword><keyword><style  face="normal" font="default" size="100%">In Vitro Techniques</style></keyword><keyword><style  face="normal" font="default" size="100%">Protein Denaturation</style></keyword><keyword><style  face="normal" font="default" size="100%">Superoxide Dismutase</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1975</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1975 Sep-Oct</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">20</style></volume><pages><style face="normal" font="default" size="100%">783-7</style></pages><language><style face="normal" font="default" size="100%">rus</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Optical and ESR spectra of erythrocyte superoxide dismutase denaturated with acid and alkali are described. Sharp changes in activity and spectra were found. &quot;Residual&quot; activity of alkaline denaturated protein was higher than of acidic denaturated sample. It is suggested that covalent bonding copper-nitrogen is essential for superoxide dismutase activity of the protein or synthetic copper complexes.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1099?dopt=Abstract</style></custom1></record></records></xml>