نتایج جستجو برای: superoxide dismutases
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The major superoxide dismutase ("slow" electromorph) of the fruit fly, Drosophila melanogaster, has been purified to homogeneity. This enzyme contains 2 Cu2+ and 2 Zn2+/molecule. The ultraviolet absorption spectrum indicates a lack of tryptophan. This enzyme has a molecular weight of 32,000 and is composed of two subunits of equal size, which are joined by noncovalent interactions. Cyanide at 1...
A group of Cu,Zn-superoxide dismutases from pathogenic bacteria is characterized by histidine-rich N-terminal extensions that are in a highly exposed and mobile conformation. This feature allows these proteins to be readily purified in a single step by immobilized metal affinity chromatography. The Cu,Zn-superoxide dismutases from both Haemophilus ducreyi and Haemophilus parainfluenzae display ...
A series of mutant human and yeast copper-zinc superoxide dismutases has been prepared, with mutations corresponding to those found in familial amyotrophic lateral sclerosis (ALS; also known as Lou Gehrig's disease). These proteins have been characterized with respect to their metal-binding characteristics and their redox reactivities. Replacement of Zn2+ ion in the zinc sites of several of the...
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