Geoffrey crabb (19 Ergebnisse)

Zustand: Good. Former library copy. Pages intact with minimal writing/highlighting. The binding may be loose and creased. Dust jackets/supplements are not included. Includes library markings. Stock photo provided. Product includes identifying sticker. Better World Books: Buy Books. Do Good.

Zustand: Good. Former library copy. Pages intact with minimal writing/highlighting. The binding may be loose and creased. Dust jackets/supplements are not included. Includes library markings. Stock photo provided. Product includes identifying sticker. Better World Books: Buy Books. Do Good.

Hardcover. Zustand: Very Good. Very good condition hard cover, some wear to cover and spine, internally clean and tidy with unmarked pages, in a good readable condition.

Zustand: Good. First edition (softcover). 8vo (23cm by 16cm), 104pp. Illustrated throughout in b&w. Original laminated card wrappers. There is some creasing of the covers; overall, this book is in good condition. ISBN.

hardcover. Zustand: Very Good.

Zustand: New. In English.

Zustand: New. In English.

Paperback. Zustand: Brand New. 616 pages. 9.61x6.69x1.40 inches. In Stock.

Taschenbuch. Zustand: Neu. Druck auf Anfrage Neuware - Printed after ordering - The Sixth International Workshop on the Enzymology and Molecular Biology of Carbonyl Metabolism was held outside of Dublin, Ireland at the end of June, 1992. Prof. Keith Tipton, Chairman of the Biochemistry Department at Trinity College, kindly agreed to host the meeting. On behalf of all of us who attended I wish to extend our sincere thanks to the whole Tipton family for making us feel so welcome in Ireland. It has been a decade since the frrst workshop was held in Bern, Switzerland. The scope of the meetings reflected somewhat the changes that have occurred in biochemistry during the past decade. At the first meeting primarily enzymes and their properties were discussed. At this last meeting many of the talks centered on gene regulation as well as more traditional aspects of enzymology and metabolism. During the past decade site directed mutagenesis to probe for the active site of an enzyme has become part of traditional enzymology; this was virtually unheard of at our frrst meeting. Many of the presenters now used this tool to study some aspect of structure and function of one of the three carbonyl metabolizing enzymes.…

Zustand: New. In English.

Taschenbuch. Zustand: Neu. Enzymology and Molecular Biology of Carbonyl Metabolism 6 | Henry Weiner (u. a.) | Taschenbuch | xiv | Englisch | 2013 | Humana | EAN 9781461376927 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu. …

Zustand: New. In English.

Gebunden. Zustand: New.

Gebunden. Zustand: New. Aldehyde Dehydrogenase. Crystal Structure of a Class 3 Aldehyde Dehydrogenase at 2.6 angstrom Resolution Z-J. Liu, et al. Conserved Residues in the Aldehyde Dehydrogenase Family: Locations in the Class 3 Tertiary Structure J. Hempel, et al. Class 3 Aldehy.

Zustand: Good. 616 pp., Hardcover, ex library, else text clean and binding tight. - If you are reading this, this item is actually (physically) in our stock and ready for shipment once ordered. We are not bookjackers. Buyer is responsible for any additional duties, taxes, or fees required by recipient's country. Photos available upon request.…

Hardcover. Zustand: Brand New. 602 pages. 10.50x7.00x1.50 inches. In Stock.

Hardcover. Zustand: Brand New. 632 pages. 10.25x6.50x1.25 inches. In Stock.

Buch. Zustand: Neu. Neuware - Aldehyde Dehydrogenase. Crystal Structure of a Class 3 Aldehyde Dehydrogenase at 2.6angstrom Resolution; Z-J. Liu, et al. Conserved Residues in the Aldehyde Dehydrogenase Family: Locations in the Class 3 Tertiary Structure; J. Hempel, et al. Class 3 Aldehyde Dehydrognease: A View from the Hills; R. Lindahl, et al. Human Corneal and Lens Aldehyde Dehydrogenases: Purification and Properties of Human Lens ALDH1 and Differential Expression as Major Soluble Proteins in Human Lens (ALDH1) and Cornea (ALDH3); G. King, R. Holmes. Alcohol Dehydrogenase. Alcohol Dehydrogenase Variability: Evolutionary and Functional Conclusions from Characterization of Further Variants; H. Jörnvall, et al. Three-Dimensional Structures of Human Alcohol Dehydrogenase Isoenzymes Reveal the Molecular basis for Their Functional Diversity; T.D. Hurley, et al. Mammalian Class II Alcohol Dehydrogenase: A Highly Variable Enzyme; J.-O. Höög, S. Svensson. Activity of Liver Alcohol Dehydrogenases on Steroids; D.K. Wilson, et al. Aldo/Keto Reductases. Structural Studies of Aldo-Keto Reductase Inhibition; D.K. Wilson, et al. Aldehyde Reductase: Catalytic Mechanism and Substrate Recognition; O.A. Barski, et al. Study of Non-Covalent Enzyme-Inhibitor Complexes of Aldose Reductase by Electrospray Mass Spectrometry; N. Potier, et al. 55 Additional Articles. Index.…

Buch. Zustand: Neu. Neuware - Aldehyde Dehydrogenases-The 1992 Perspective.- Metabolic Role of Aldehyde Dehydrogenase.- Effects of Aldehyde Products of Lipid Peroxidation on the Activity of Aldehyde Metabolizing Enzymes in Hepatomas.- Metabolic Interactions of 4-Hydroxynonenal, Acetaldehyde and Glutathione in Isolated Liver Mitochondria.- Biological Role of Human Cytosolic Aldehyde Dehydrogenase 1: Hormonal Response, Retinal Oxidation and Implication in Testicular Feminization.- Human Cytosolic Aldehyde Dehydrogenase in Androgen Insensitivity Syndrome.- The Use of Immortalized Mouse L1210/OAP Cells Established in Culture to Study the Major Class 1 Aldehyde Dehydrogenase-Catalyzed Oxidation of Aldehydes in Intact Cells.- Enhanced Transcription of the Cytosolic ALDH Gene in Cyclophosphamide Resistant Human Carcinoma Cells.- Attempts to Increase the Expression of Rat Liver Mitochondrial Aldehyde Dehydrogenase in E. coli by Altering the mRNA.- Preliminary Characterization of the Rat Class 3 Aldehyde Dehydrogenase Gene.- Human High-Km Aldehyde Dehydrogenase (ALDH3): Molecular, Kinetic, and Structural Features.- Overexpression or Polycyclic Aromatic Hydrocarbon-Mediated Induction of an Apparently Novel Class 3 Aldehyde Dehydrogenase in Human Breast Adenocarcinoma Cells and Its Relationship to Oxazaphosphorine-Specific Acquired Resistance.- Tumor-Associated Aldehyde Dehydrogenase (ALDH3): Expression in Different Human Tumor Cell Lines with and without Treatment with 3-Methylcholanthrene.- Sexual Differentiation in the Induction of the Class 3 Aldehyde Dehydrogenase.- Mouse Class 3 Aldehyde Dehydrogenases: Positive and Negative Regulation of Gene Expression.- Human Stomach Aldehyde Dehydrogenase, ALDH3.- Bovine Corneal Aldehyde Dehydrogenases: Evidence for Multiple Gene Products (ALDH3 and ALDHX).- Carbonyl-Metabolizing Enzymes and Their Relatives Recruited as Structural Proteins in the Eye Lens.- Members of the ALDH Gene Family are Lens and Corneal Crystalline.- Retinoic Acid Synthesis in the Developing Retina.- Human Liver High Km Aldehyde Dehydrogenase (ALDH4): Properties and Structural Relationship to the Yeast Glutamic -Semialdhyde Dehydrogenase.- Effect of Some Compounds Related to Disulfiram on Mitochondrial Aldehyde Dehydrogenase in Vitro and in Vivo.- Photoaffinity Labeling of Aldehyde Dehydrogenase from Horse Liver by P1-N6-(4-Azidophenylethyl) Adenosine-P2[4-(3-Azidopyridinio)Butyl] Diphosphate.- Aldehyde Dehydrogenase: Aldehyde Dehydrogenation and Ester Hydrolysis.- Is the Single Site Binding Model for Aldehyde Dehydrogenase an Oversimplification The One-Site, Two-Site Debate Revisited.- Crystallization and Preliminary X-Ray Analysis of Bovine Mitochondrial Aldehyde Dehydrogenase and Human Glutathione-Dependent Formaldehyde Dehydrogenase.- Aldo-Keto Reductases: An Overview.- Location of an Essential Arginne Residue in the Primary Structure of Pig Aldose Reductase.- Cys298 Is Responsible for Reversible Thiol-Induced Variation in Aldose Reductase Activity.- Substrate Specificity of Reduced and Oxidized Forms of Human Aldose Reductase.- Kinetic Alteration of Human Aldose Reductase by Mutagenesis of Cysteine Residues.- Inhibition of Aldose Reductase by (2, 6-Dimethylphenylsulphonyl) Nitromethane: Possible Implications for the Nature of an Inhibitor Binding Site and a Cause of Biphasic Kinetics.- Sepiapterin Reductase and ALR2 ('Aldose Reductase') from Bovine Brain.- Polymorphisms of the Aldose Reductase Locus (ALR2) and Suseptibility to Diabetic Microvascular Complications.- Polycyclic Aromatic Hydrocarbons and Phenolic Antioxidants do not Significantly Induce Carbonyl Reductase in Human Cell Lines.- The Purification and Properties of a Novel Carbonyl Reducing Enzyme from Mouse Liver Microsomes.- Properties and Stereoselectivity of Carbonyl Reductases Involved in the Ketone Reduction of Warfarin and Analogues.- Activation of Pulmonary Carbonyl Reductase by Aromatic Amines and Pyridine Ring-Containing Compounds.- Unique Dihydrodiol Specific Dehydr.…