Protein Crosslinking: Biochemical and Molecular Aspects: Advances in Experimental Medicine and Biology, cartea 86A
Autor Mendel Friedmanen Limba Engleză Paperback – 12 dec 2012
Toate formatele și edițiile | Preț | Express |
---|---|---|
Paperback (2) | 427.04 lei 6-8 săpt. | |
Springer Us – 12 dec 2012 | 427.04 lei 6-8 săpt. | |
Springer Us – 27 iun 2013 | 668.36 lei 6-8 săpt. |
Din seria Advances in Experimental Medicine and Biology
- 9% Preț: 719.56 lei
- 5% Preț: 717.20 lei
- 20% Preț: 691.93 lei
- 5% Preț: 715.71 lei
- 5% Preț: 1113.83 lei
- 5% Preț: 1031.00 lei
- 15% Preț: 640.24 lei
- 5% Preț: 717.00 lei
- 5% Preț: 820.42 lei
- 5% Preț: 717.00 lei
- 5% Preț: 715.35 lei
- 5% Preț: 716.28 lei
- 5% Preț: 716.28 lei
- 15% Preț: 641.38 lei
- 20% Preț: 1161.71 lei
- 5% Preț: 1170.51 lei
- 18% Preț: 1119.87 lei
- 5% Preț: 1288.48 lei
- 5% Preț: 1164.67 lei
- 5% Preț: 1101.73 lei
- 18% Preț: 1123.67 lei
- 5% Preț: 1435.64 lei
- 20% Preț: 1044.10 lei
- 18% Preț: 946.39 lei
- 5% Preț: 292.57 lei
- 18% Preț: 957.62 lei
- 18% Preț: 1235.76 lei
- 5% Preț: 1231.55 lei
- 5% Preț: 1292.30 lei
- 5% Preț: 1102.10 lei
- 18% Preț: 1132.81 lei
- 5% Preț: 1165.19 lei
- 5% Preț: 1418.48 lei
- 5% Preț: 1305.63 lei
- 18% Preț: 1417.72 lei
- 18% Preț: 1412.99 lei
- 24% Preț: 806.15 lei
- 18% Preț: 1243.29 lei
- 5% Preț: 1429.44 lei
- 5% Preț: 1618.70 lei
- 5% Preț: 1305.12 lei
- 18% Preț: 1124.92 lei
- 5% Preț: 1097.54 lei
- 15% Preț: 649.87 lei
- 5% Preț: 1097.54 lei
- 18% Preț: 945.79 lei
- 5% Preț: 1123.13 lei
- 20% Preț: 816.43 lei
Preț: 427.04 lei
Nou
Puncte Express: 641
Preț estimativ în valută:
81.72€ • 83.69$ • 67.98£
81.72€ • 83.69$ • 67.98£
Carte tipărită la comandă
Livrare economică 18 martie-01 aprilie
Preluare comenzi: 021 569.72.76
Specificații
ISBN-13: 9781468432848
ISBN-10: 1468432842
Pagini: 784
Ilustrații: XX, 760 p. 66 illus.
Dimensiuni: 178 x 254 x 41 mm
Greutate: 1.33 kg
Ediția:Softcover reprint of the original 1st ed. 1977
Editura: Springer Us
Colecția Springer
Seria Advances in Experimental Medicine and Biology
Locul publicării:New York, NY, United States
ISBN-10: 1468432842
Pagini: 784
Ilustrații: XX, 760 p. 66 illus.
Dimensiuni: 178 x 254 x 41 mm
Greutate: 1.33 kg
Ediția:Softcover reprint of the original 1st ed. 1977
Editura: Springer Us
Colecția Springer
Seria Advances in Experimental Medicine and Biology
Locul publicării:New York, NY, United States
Public țintă
ResearchCuprins
of Part A.- 1. Biologically Important Thiol-Disulfide Reactions and the Role of Cyst(e)ine in Proteins: an Evolutionary Perspective.- 2. Disulfide Crosslinks and the Specificity of Protein Turnover in Plants.- 3. Protein Thiol-Disulfide Interchange and Interfacing with Biological Systems.- 4. on the Mechanism of Renaturation of Proteins Containing Disulfide Bonds.- 5. Disulfide Bonds: Key to Wheat Protein Functionality.- 6. Chemical Strategy for Studying the Antigenic Structures of Disulfide-Containing Proteins: Hen Egg-White Lysozyme as a Model.- 7. Crosslinking of Antibody Molecules by Bifunctional Antigens.- 8. Modification of the Biological Properties of Plant Lectins by Chemical Crosslinking.- 9. Introduction of Artificial Crosslinks Into Proteins.- 10. Synthesis and Application of new Bifunctional Reagents.- 11. Synthesis and Application of Cleavable and Hydrophilic Crosslinking Reagents.- 12. Comparison of Hydrophobic and Strongly Hydrophilic Cleavable Crosslinking Reagents in Intermolecular Bond Formation in Aggregates of Proteins Or Protein-Rna.- 13. Crosslinking of Ribosomes by Cleavable Bifunctional Mercaptoimidates.- 14. on the Introduction of Disulfide Crosslinks Into Fibrous Proteins and Bovine Serum Albumin.- 15. Thiolation and Disulfide Cross-Linking of Insulin to Form Mac Romolecules of Potential Therapeutic Value.- 16. Crosslinked Insulins: Preparation, Properties and Applications.- 17. the Enzymic Derivation of Citrulline Residues From Arginine Residues in Situ During the Biosynthesis of Hair Proteins That Are Cross-Linked by Isopeptide Bonds.- 18. Thermodynamics of Crosslinks.- 19. Physical and Chemical Consequences of Keratin Crosslinking, with Application to the Determination of Crosslink Density.- 20. An X-Ray Diffraction Study of Thermally-Induced Structural Changes in ?-Keratin.- 21. Introduction of new Crosslinks Into Proteins.- 22. Comparison of Wool Reactions with Selected Monoand Bifunctional Reagents.- 23. the effects of Ethylene Glycol on Wool Fibers.- 24. Protein: Polyanion Interactions. Studies of the Trehalose-P Synthetase as a Model System.- 25. Kinetic Studies of Immobilized ?-Chymotrypsin in Apolar Solvents.- 26. Factors Affecting Cyanoborohydride Reduction of Aromatic Schiff’S Bases in Proteins.- 27. Chemistry of the Crosslinking of Collagen During Tanning.- 28. Chemical Modification of Collagen and the effects on Enzyme-Binding: Mechanistic Considerations.- 29. Strategies in the Racemization-Free Synthesis of Polytripeptide Models of Collagen.- 30. Conformational Properties of Polypeptide Models of Collagen.- 31. Ionizing Radiation-Induced Crosslinking in Proteins.- 32. Peroxydisulfate Anion-Induced Crosslinking of Proteins.- 33. Cross Linking in the Radiolysis of some Enzymes and Related Proteins.- 34. Isolation and Characterization of Stable Protein-DNA Adducts Induced in Chromatin by Ultraviolet Light.- 35. Identification of Binding Sites of the E. Coli Ribosome by Affinity Labeling.- 36. Photoinduced Nucleic Acid-Protein Crosslinkage in Ribosomes and Ribosome Complexes.- 37. Crosslinking of Nucleic Acids and Proteins by Bisulfite.- 38. Crosslinking of Amino Acids by Formaldehyde. Preparation and 13C Nmr Spectra of Model Compounds.- 39. Electron Microscopy of An Oligomeric Protein Stabilized by Poly Functional Cross-Linking.- 40. Fish Myofibrillar Protein and Lipid Interaction in Aqueous Media as Derived by Isotope Labeling, Sucrose Gradient Centrifugation, Polyacrylamide Electrophoresis and Electron Paramagnetic Resonance.- 41. Gas-Liquid Chromatography and Mass Spectrometry ofLanthionine, Lysinoalanine, and S-Carboxy-Ethylcysteine.- 42. Mass Spectra of Cysteine Derivatives.- 43. a Nuclear Magnetic Double Resonance Study of N-?-Bis(?’-Chloroethyl)Phosphonylethyl-DL-Phenylalanine.