marc maire (25 risultati)

Condizione: As New. Envoi rapide Etat de Neuf. in8. 2012. Broché. 148 pages. As New.

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Encuadernación de tapa blanda. Condizione: Bien. 1ª Edición. ´142 p. ; 18x12 cms., retrs. Proyectó la edición Mauricio Amster. Problemas de Nuestro Tiempo, Colección Cormorán (OC-Amster ).

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Taschenbuch. Condizione: Neu. Laboratory Guide to Biochemistry, Enzymology, and Protein Physical Chemistry | A Study of Aspartate Transcarbamylase | Marc Le Maire (u. a.) | Taschenbuch | xii | Englisch | 2012 | Springer | EAN 9781461367048 | Verantwortliche Person für die EU: Springer Verlag GmbH, Tiergartenstr. 17, 69121 Heidelberg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.

Taschenbuch. Condizione: Neu. Druck auf Anfrage Neuware - Printed after ordering - The study of a single well-chosen substance, here aspartate transcarb amylase, can provide an excellent basis for a laboratory course. The student is introduced to a variety of scientific ideas and to many experi mental and interpretive techniques. This enzyme is readily available, is relatively stable, has an extensive literature, and its behavior has many facets: substrate inhibition, a large change in structure upon homo tropic activation by substrates, allosteric stimulation by ATP, allosteric inhibition by CTP synergistic with VTP, positive cooperativity for sub strates, negative cooperativity for CTP binding, and dissociation and reassembly of subunits Cand R2 from the holoenzyme CI5. In addition 3 6 to the known biochemical aspects of these properties, the results ob tained here can be interpreted in the light of the high-resolution X-ray diffraction structures of the T and R forms, the low-angle X-ray scattering results, and the large number of mutants now available by recombinant DNA methods. Future development of this course could also involve part of these methods, as well as the carefully chosen experiments described here. This approach resembles research more than the approaches one usually finds in biochemical laboratory courses. A consistent develop ment of ideas about a single enzyme, which shows so many facets in its behavior, is sure to hold the interest of the student. Moreover, one explores a depth, and reasons to move forward, that are an essential part of research.

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Paperback. Condizione: Brand New. 184 pages. 9.00x6.25x0.50 inches. In Stock.

Condizione: New. KlappentextThis guide for a laboratory course presents an integrated set of experiments relying entirely on the use of unique enzyme, aspartate transcarbamylase, which exhibits all of the catalytic and regulatory properties characteristi.

Taschenbuch. Condizione: Neu. Neuware - 1 Aspartate Transcarbamylase.- 2 Molecular Genetics: Regulation of Aspartate Transcarbamylase Biosynthesis.- 3 Purification of Aspartate Transcarbamylase and Its Subunits.- 4 Structural and Physicochemical Study of Aspartate Transcarbamylase.- 5 Enzymatic Catalysis and Regulation.- 6 Complementary Experiments.- 1. Equations and Units.- 2. Molar Mass and Molecular Mass.- 3. Units of Catalytic Activity.- 4. Units of Radioactivity.- 5. Units of Quantity.- 7. Calculation of Acceleration.- 8. Bacterial Strains.- 9. Solutions and Reagents.- 9.1. 0.8-M Tris-Acetate Buffer, pH 8.- 9.2. 0.2-M Acetic Acid.- 9.6. Elution Buffer for Chromatography: 10 × Stock Solution.- 9.7. 100-mM Aspartate, pH 8.- 9.8. 10-mM Carbamylaspartate, pH 8.- 9.9. 1-M Phosphate Buffer, pH 7.2.- 9.10. Buffer for Dilution of E.- 9.11. Buffer for Dilution of C.- 9.12. Buffer for Dilution of R and Recombination.- 9.13. 200-mM Cacodylate Buffer, pH 6, 7, and 7.5.- 9.14. 200-mM Tris-Acetate Buffer, pH 8 and 9.- 9.15. 200-mM Glycine Buffer, pH 10.- 9.16. 400-mM Succinate, pH 7.- 9.17. Reaction Medium: 20-mM CAP-200-mM Tris-Acetate, pH 8.- 10. Preparation of Standard Protein Mixtures for Column Calibration.- Answers To Questions.- References.

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Couverture souple. Condizione: Bon. Edition originale. Genève 1961. 1 Volume/1. Broché cousu. Format in-8°( 24 x 16,5 cm )( 1180 gr ). ------- 677 pages et quelques illustrations. ******************** Mémoires et Documents Tome XL ***************** Textes de : Marc-R. Sauter - Louis Dupraz - Paul Rousset - François-L. Ganshof - Robert Fawtier - Carl-J. Bruckhardt - Emile-G. Léonard - Jacques Freymond - André Gür - Iso Müller - W. Amédée Liebeskind - Sven Stelling-Michaud - Anton Largiadèr - André Donnet - Hektor Ammann - Colin Martin - Louis Junod - Paul Roth - Paul-F. Geisendorf - Jean-Charles Biaudet - Bernard Cuénoud - Edgar Bonjour - Léon Kern - Louis Blondel - Bernard Gagnebin - Robert Avezou - Louis Binz - Antony Babel - Gustave Vaucher - Henri Meylan - Jean-François Bergier - Paul Chaix - Alain Dufour - Henri Delaurue - Olivier Reverdin - Anne-M. Piuz - Jaques Couvoisier - Jean-Daniel Candaux - Frédéric Barbey - Paul Guichonnet - Marguerite Maire - Jean-Claude Frachebourg - Luc Monnier - Marc Vuilleumier - Maurice Battelli. ****************** ref att 980.

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Taschenbuch. Condizione: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -The study of a single well-chosen substance, here aspartate transcarb amylase, can provide an excellent basis for a laboratory course. The student is introduced to a variety of scientific ideas and to many experi mental and interpretive techniques. This enzyme is readily available, is relatively stable, has an extensive literature, and its behavior has many facets: substrate inhibition, a large change in structure upon homo tropic activation by substrates, allosteric stimulation by ATP, allosteric inhibition by CTP synergistic with VTP, positive cooperativity for sub strates, negative cooperativity for CTP binding, and dissociation and reassembly of subunits Cand R2 from the holoenzyme CI5. In addition 3 6 to the known biochemical aspects of these properties, the results ob tained here can be interpreted in the light of the high-resolution X-ray diffraction structures of the T and R forms, the low-angle X-ray scattering results, and the large number of mutants now available by recombinant DNA methods. Future development of this course could also involve part of these methods, as well as the carefully chosen experiments described here. This approach resembles research more than the approaches one usually finds in biochemical laboratory courses. A consistent develop ment of ideas about a single enzyme, which shows so many facets in its behavior, is sure to hold the interest of the student. Moreover, one explores a depth, and reasons to move forward, that are an essential part of research. 184 pp. Englisch.

Taschenbuch. Condizione: Neu. This item is printed on demand - Print on Demand Titel. Neuware -The study of a single well-chosen substance, here aspartate transcarb amylase, can provide an excellent basis for a laboratory course. The student is introduced to a variety of scientific ideas and to many experi mental and interpretive techniques. This enzyme is readily available, is relatively stable, has an extensive literature, and its behavior has many facets: substrate inhibition, a large change in structure upon homo tropic activation by substrates, allosteric stimulation by ATP, allosteric inhibition by CTP synergistic with VTP, positive cooperativity for sub strates, negative cooperativity for CTP binding, and dissociation and reassembly of subunits Cand R2 from the holoenzyme CI5. In addition 3 6 to the known biochemical aspects of these properties, the results ob tained here can be interpreted in the light of the high-resolution X-ray diffraction structures of the T and R forms, the low-angle X-ray scattering results, and the large number of mutants now available by recombinant DNA methods. Future development of this course could also involve part of these methods, as well as the carefully chosen experiments described here. This approach resembles research more than the approaches one usually finds in biochemical laboratory courses. A consistent develop ment of ideas about a single enzyme, which shows so many facets in its behavior, is sure to hold the interest of the student. Moreover, one explores a depth, and reasons to move forward, that are an essential part of research.Springer-Verlag KG, Sachsenplatz 4-6, 1201 Wien 184 pp. Englisch.

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