MARC Record from marc_columbia

LEADER: 03751fam a2200349 a 4500
001 2288226
005 20220616012128.0
008 980616t19991999nyua b 001 0 eng
010 $a 98028908
020 $a0471242446 (cloth : alk. paper)
035 $a(OCoLC)39323127
035 $a(OCoLC)ocm39323127
035 $9APD6920CU
035 $a(NNC)2288226
035 $a2288226
040 $aDLC$cDLC$dDLC$dOrLoB-B
050 00 $aQP603.P4$bD86 1999
082 00 $a572/.791$221
100 1 $aDunford, H. Brian.$0http://id.loc.gov/authorities/names/n82070358
245 10 $aHeme peroxidases /$cH. Brian Dunford.
260 $aNew York :$bJohn Wiley,$c[1999], ©1999.
300 $axiii, 507 pages :$billustrations ;$c25 cm
336 $atext$btxt$2rdacontent
337 $aunmediated$bn$2rdamedia
504 $aIncludes bibliographical references and index.
505 00 $g1.$tIntroduction. Historical Background --$g2.$tModel Peroxidases from Yeast and Horseradish, Cloned Enzymes, and Comparison to Metmyoglobin --$g3.$tHeme Peroxidase and Catalase Families and Superfamilies: Crystal Structures --$g4.$tHorseradish Peroxidase. I: Ligand Binding, Redox Potentials, Formation of Its Compounds, and Some of Their Reactions --$g5.$tHorseradish Peroxidase. II: Isoenzymes, Steady-State Kinetics, and Peroxidase-Oxidase Reaction --$g6.$tHorseradish Peroxidase. III: Reaction with Indole-3-Acetic Acid, Light Emission, and Quantitative Structure-Activity Relationships --$g7.$tSpectroscopy of Horseradish Peroxidase. I: Optical, Resonance Raman, Magnetic Circular Dichroism, X-ray Absorption, and Diffraction --$g8.$tSpectroscopy of Horseradish Peroxidase. II: Nuclear Magnetic Resonance, Electron Paramagnetic Resonance, Electron Nuclear Double Resonance, Mossbauer Spectroscopy, and Theoretical Studies --$g9.$tYeast Cytochrome c Peroxidase. I: Properties and Reactions with Small Molecules --
505 80 $g10.$tYeast Cytochrome c Peroxidase. II: Interaction with Cytochrome c --$g11.$tOther Class I Peroxidases: Ascorbate Peroxidase and Bacterial Catalase-Peroxidases --$g12.$tClass II Peroxidases: Lignin, Manganese, and Coprinus cinereus Peroxidases --$g13.$tOther Class III Plant Peroxidases: Peanut, Barley, Tobacco, and Arabidopsis thaliana --$g14.$tChloroperoxidase and Pseudomonas Cytochrome c Peroxidase --$g15.$tMyeloperoxidase and Eosinophil Peroxidase: Phagocytosis and Microbial Killing --$g16.$tProstaglandin Endoperoxide H Synthases --$g17.$tLactoperoxidase, Thyroid Peroxidase, and Other Animal Peroxidases --$g18.$tCatalases.
520 $aThis book reflects the tremendous growth peroxidases research has experienced in recent years, providing for the first time in over three decades a systematic, up-to-date treatment of the subject.
520 8 $aFrom cancer in plants to unique saddle-shaped hemes in peroxidases, it consolidates vast amounts of information previously scattered in the professional literature, covering all aspects of these ubiquitous enzymes that act on a variety of substances and processes in living systems - their properties, reactions, crystal structures, cloning, and more.
520 8 $aThis one-stop reference for analytical biochemists, biotechnologists, and others interested in the study and use of peroxidases, offers a critical review of the literature, and sorts through the various conflicting reports about peroxidase mechanisms. It familiarizes the reader with commercial and industrial applications in analytical biochemistry, biotechnology, medicine, agriculture, and the environmentaddressing future trends in drug synthesis, water purification, and soil decontamination.
650 0 $aPeroxidase.$0http://id.loc.gov/authorities/subjects/sh85100032
852 00 $boff,bio$hQP603.P4$iD86 1999