Friedman | Protein Crosslinking | Buch | 978-1-4757-9115-0 | www2.sack.de

Buch, Englisch, 740 Seiten, Format (B × H): 170 mm x 244 mm, Gewicht: 1293 g

Reihe: Advances in Experimental Medicine and Biology

Friedman

Protein Crosslinking

Nutritional and Medical Consequences
Erscheinungsjahr 2013
ISBN: 978-1-4757-9115-0
Verlag: Springer

Nutritional and Medical Consequences

Buch, Englisch, 740 Seiten, Format (B × H): 170 mm x 244 mm, Gewicht: 1293 g

Reihe: Advances in Experimental Medicine and Biology

ISBN: 978-1-4757-9115-0
Verlag: Springer


The word crosslinking implies durable combination of usually large, distinct elements at specific places to create a new entity that has different properties as a result of the union. In the case of proteins, such crosslinking often results in important changes in chemical, physical, functional, nutritional, and biome dical properties, besides physical properties simply related to molecular size and shape. (Nucleic acids, carbohydrates~ glyco proteins, and other biopolymers are correspondingly affected.) Since proteins are ubiquitous, the consequences of their crosslin king are widespread and often profound. Scientists from many dis ciplines including organic chemistry, biochemistry, protein chemis try, food science, nutrition, radiation biology, pharmacology, physiology, medicine, and dentistry are, therefore, very much inte rested in protein crosslinking reactions and their implications. Because protein crosslinking encompasses so many disciplines, in organizing the Symposium on Nutritional and Biochemical Consequences of Protein Crosslinking sponsored by the Protein Subdivision of the Division of Agricultural and Food Chemistry of the American Chemical Society, I sought participants with the broadest possible range of interests, yet with a common concern for theoretical and practical aspects of protein crosslinking. An important function of a symposium is to catalyze progress by bringing together ideas and experiences needed for interaction among different, yet related disciplines. To my pleasant surprize, nearly everone invited came to San Francisco to participate.

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of Part B.- 1. Crosslinking Amino Acids Nomenclature — Stereochemistry and Nomenclature.- 2. Biological Effects of Alkali-Treated Protein and Lysinoalanine: An Overview.- 3. Editor’s Note.- 4. Metabolic Transit of Lysinoalanine (LAL) Bound to Protein and of Free Radioactive [14C]-Lysinoalanine.- 5. Lysinoalanine Formation in Protein Food Ingredients.- 6. Inhibitory Effect of Mercaptoamino Acids on Lysinoalanine Formation During Alkali Treatment of Proteins.- 7. Cystine-Alkali Reactions in Relation to Protein Crosslinking.- 8. New Amino Acid Derivatives Formed By Alkaline Treatment of Proteins.- 9. ?,?-Unsaturated and Related Amino Acids in Peptides And Proteins.- 10. Behavior of O-Glycosyl and O-Phosphoryl Proteins in Alkaline Solution.- 11. 35S-Sulfide Incorporation During Alkaline Treatment of Keratin and Its Relation to Lanthionine Formation.- 12. Lysinoalanine Formation in Wool After Treatments with Some Phosphate Salts.- 13. The Formation and Cleavage of Lysinoalanine Crosslinks.- 14. On the Specific Cleavage of Cysteine Containing Peptides and Proteins.- 15. Reactions of Proteins with Dehydroalanines.- 16. Nutritional Significance of Crosslink Formation During Food Processing.- 17. The Formation, Isolation and Importance of Isopeptides in Heated Proteins.- 18. Heat Induced Crosslinks in Milk Proteins and Consequences for the Milk System.- 19. The Complete Enzymic Hydrolysis of Crosslinked Proteins.- 20. Cross-Linking of Protein by Peroxidase.- 21. A Mathematical Analysis of Kinetics of Consecutive, Competitive Reactions of Protein Amino Groups.- 22. Effect of Maillard Browning Reaction on Nutritional Quality of Protein.- 23. Availability of the True Schiff’s Bases of Lysine. Chemical Evaluation of the Schiff’s Base Between Lysine and Lactose in Milk.-24. The Biological Significance of Carbohydrate-Lysine Crosslinking During Heat-Treatment of Food Proteins.- 25. The Physical Aspects with Respect to Water and Non-Enzymatic Browning.- 26. Oxidative Browning of Amadori Compounds from Amino Acids And Peptides.- 27. The Possible Utilization of the 1-Amino-I-Deoxy-2-Ketose Compounds Between Amino Acids and Carbohydrates as Foodstuff Integrators.- 28. Novel Free Radicals Formed by the Amino-Carbonyl Reactions of Sugars with Amino Acids, Amines, and Proteins.- 29. Some Chemical and Nutritional Properties of Feather Protein Isolates Containing Varying Half-Cystine Levels.- 30. Effect of Processing on Protein Utilization by Ruminants.- 31. Protected Proteins in Ruminant Nutrition. Invitro Evaluation of Casein Derivatives.- 32. Protein Interrelationships in Roughages as Affecting Ruminant Dietary Protein Adequacy.- 33. Some Therapeutic Implications of the Crosslinkage Theory of Aging.- 34. Chemistry of Collagen Crosslinking: Relationship to Aging and Nutrition.- 35. Nutritional Copper Deficiency and Penicillamine Administration: Some Effects on Bone Collagen and Arterial Elastin Crosslinking.- 36. Chemical Basis for Pharmacological and Therapeutic Actions of Penicillamine.- 37. Location of the Intermolecular Crosslinking Sites in Collagen.- 38. The Qualitative and Quantitative Crosslink Chemistry of Collagen Matrices.- 39. Studies on Cross-Linked Regions of Elastin.



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