By Alton Meister
Advances in Enzymology and similar parts of Molecular Biology is a seminal sequence within the box of biochemistry, delivering researchers entry to authoritative studies of the most recent discoveries in all parts of enzymology and molecular biology. those landmark volumes date again to 1941, supplying an unmatched view of the old improvement of enzymology. The sequence bargains researchers the newest realizing of enzymes, their mechanisms, reactions and evolution, roles in advanced organic approach, and their program in either the laboratory and undefined. each one quantity within the sequence positive aspects contributions through major pioneers and investigators within the box from around the globe. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.
With its wide selection of themes and lengthy historic pedigree, Advances in Enzymology and comparable parts of Molecular Biology can be utilized not just by way of scholars and researchers in molecular biology, biochemistry, and enzymology, but additionally by means of any scientist drawn to the invention of an enzyme, its houses, and its functions.
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Extra info for Advances in Enzymology and Related Areas of Molecular Biology, Volume 41
T h e Manganese Enzyme B. T h e Ferrienzyme C. Intracellular Localization VI. Mitochondria1 Superoxide Dismutase A. Intracellular Distribution B. Intramitochondrial Localization C . Site of Synthesis D. Evolutionary Significance VII. Biological Importance of Superoxide Dismutase A. Distribution Studies B. Mutants C . Induction of the Enzyme D. Oxygen Toxicity E. Oxygen-Streptonigrin Synergism F. T h e Iron Superoxide Dismutase VIII. Superoxide Dismutase as a Probe for 0,IX. Summary and Projections References 35 36 37 37 39 41 44 44 47 51 Y 56 58 59 63 64 67 69 70 70 71 73 73 73 75 75 76 78 78 81 82 84 86 86 88 90 91 36 IRWIN FRIDOVICH I.
A positive assay for this enzyme would certainly be preferable, but, given the nature of the substrate, will not soon be available. IV. Copper-Zinc Superoxide Dismutases A . HISTORICAL BACKGROUND In 1938 Mann and Keilin (104) described a blue-green protein they had isolated from ox blood. 38% copper. Because it had no discernible activity, its name was derived from its source and content of copper, that is, hemocuprein. Its isolation, on the basis of copper content, had been undertaken because of a n interest in carbonic anhydrase coupled with the hypothesis that carbonic anhydrase might be a cuproprotein (105).
0,--The Substrate A. General Properties of 0,B. Biological Sources of 0,C. T h e Dangers of 0,111. Assays for Superoxide Dismutase A. Direct Assays B. Indirect Assays IV. Copper-Zinc Superoxide Dismutases A. Historical Background B. Sources and Isolation Procedures C . Activity and Mechanism D. Role of the Metals E. Stability F. Structure G. Isoenzymes H. Tetrazolium Oxidase V. Bacterial Superoxide Dismutases A. T h e Manganese Enzyme B. T h e Ferrienzyme C. Intracellular Localization VI. Mitochondria1 Superoxide Dismutase A.