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Altre immaginiL'univers n'est pas sourd. Pour un nouveau rapport sciences et foi.
Collectif (Christoph Theobald, Bernard Saugier, Jean Leroy, Marc Le Maire, Dominique Grésillon)
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Couverture souple. Condizione: Très bon. Paris, Bayard, 2006, in-8, broché, couverture illustrée, 396 pp.
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Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry : A Study of Aspartate Transcarbamylase
Le Maire, Marc; Maire, Marc Le; Chabaud, Raymond; Herve, Guy
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Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry : A Study of Aspartate Transcarbamylase
Le Maire, Marc; Maire, Marc Le; Chabaud, Raymond; Herve, Guy
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Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry : A Study of Aspartate Transcarbamylase
Le Maire, Marc; Maire, Marc Le; Chabaud, Raymond; Herve, Guy
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Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry : A Study of Aspartate Transcarbamylase
Le Maire, Marc; Maire, Marc Le; Chabaud, Raymond; Herve, Guy
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Altre immagini- Brossura
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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 Heidel…berg, juergen[dot]hartmann[at]springer[dot]com | Anbieter: preigu.
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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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Laboratory Guide to Biochemistry, Enzymology and Protein Physical Chemistry: A Study of Aspartate Transcarbamylase
Le Maire, Marc/ Maire, Marc Le/ Chabaud, Raymond/ Herve, Guy
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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.
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Da: AHA-BUCH GmbH, Einbeck, GermaniaAHA-BUCH GmbH
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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 Compl…ementary 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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Da: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, , GermaniaBuchWeltWeit Ludwig Meier e.K.
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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 interpr…etive 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.
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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 interpretiv…e 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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