Main description:

This volume arose originally from the complaints of the editor's students, both undergraduate and postgraduate, that there was no modern book on protein fibers which told enough about protein science and chemical tech nologies related to fibers. By and large this is probably a reasonable cri de coeur. The undergraduate on a technological course, lacking information on the basic scientific techniques used to carry out the research on which his fiber technology is based, can find it difficult to obtain this information. The pure science undergraduate often lacks knowledge of the application of these techniques in protein fiber technology. The young graduates, com mencing research related to some aspect of protein fibers, are drawn from a wide range of scientific disciplines, having been trained as biochemists, chemists, physicists, technologists, and histologists, to name but a few. Generally these new research workers pass through a preliminary "lost" period in which they have to evaluate their background in relation to the wide and differing fields of research in protein fiber science to which they are now exposed. As time goes on they then either develop a wide knowledge covering science and technology or remain in a specific part of their original discipline, with a narrow knowledge of its application in the field of the research degree they are taking.

Contents:

1 The Basis of Protein Chemistry.- 1.1. Introduction.- 1.1.1. Outline.- 1.2. Isolation of Proteins and Their Characterization by Physical Methods.- 1.2.1. Separation Procedures.- 1.2.1.1. Chromatographic Methods.- 1.2.1.2. Electrophoretic Methods.- 1.2.2. Size and Shape of Protein Molecules.- 1.2.2.1. Gel Filtration.- 1.2.2.2. Sedimentation Analysis.- 1.2.2.3. Other Physical Methods.- 1.2.3. Determination of Secondary Structure.- 1.2.3.1. Optical Rotatory Dispersion.- 1.2.3.2. Nuclear Magnetic Resonance Spectroscopy.- 1.2.3.3. Determination of Protein Structure by X-Ray Diffraction.- 1.3. Amino Acid Analysis.- 1.3.1. Preparation of the Hydrolysate.- 1.3.2. Analysis of the Hydrolysate.- 1.3.3. Separation of Amino Acids on Paper and on Thin Layers.- 1.3.4. Amino Acid Analysis by Gas Chromatography.- 1.3.5. Miscellaneous Amino Acid Determinations.- 1.3.5.1. Tryptophan.- 1.3.5.2. Cystine.- 1.3.5.3. Lanthionine and Lysinoalanine.- 1.3.5.4. Cysteic Acid.- 1.3.5.5. Total Amide Residues.- 1.4. Disulfide Bond Cleavage.- 1.4.1. Oxidation.- 1.4.2. Reduction.- 1.4.3. Sulfitolysis.- 1.4.4. Oxidative Sulfitolysis.- 1.4.5. Cyanolysis.- 1.4.6. S-Alkylation.- 1.4.7. Estimation of Cystine and Cysteine in Proteins.- 1.4.8. Differential Labeling.- 1.5. Peptide Chain Cleavage.- 1.5.1. Cleavage by Enzymes.- 1.5.2. Cleavage by Enzymes Acting on Modified Proteins.- 1.5.2.1. Modification of Lysine.- 1.5.2.2. Modification of Arginine.- 1.5.2.3. S-Aminoethylation of Half-Cystine Residues.- 1.5.3. Cleavage by Chemical Methods.- 1.5.3.1. Cleavage at Methionine.- 1.5.3.2. Cleavage at Tryptophan and Tyrosine.- 1.5.3.3. N?O Acyl Shift: Cleavage at Serine and Threonine.- 1.5.3.4. Splitting Out Aspartic Acid with Dilute Acid.- 1.5.3.5. Hydrolysis with Concentrated Hydrochloric Acid.- 1.6. Separation of Mixtures of Peptides Produced by Chain Cleavage.- 1.6.1. Column Chromatography.- 1.6.1.1. Detection of Peptides in Effluents from Chromatographic Columns.- 1.6.2. Desalting of Peptides.- 1.6.3. Separation of Peptides on Paper.- 1.6.4. Diagonal Electrophoresis.- 1.7. Amino-Acid-Sequence Determination.- 1.7.1. N-Terminal Residues.- 1.7.1.1. l-Fluoro-2,4-dinitrobenzene(FDNB).- 1.7.1.2. Cyanate Method.- 1.7.1.3. l-Dimethylaminonaphthalene-5-Sulfonyl Chloride (Dansyl Chloride).- 1.7.1.4. Edman Degradation.- 1.7.1.5. N-Terminal-Sequence Determination with Leucine Aminopeptidase.- 1.7.1.6. Blocked N-Terminal Residues.- 1.7.2. C-Terminal Residues.- 1.7.2.1. Chemical Methods.- 1.7.2.2. Enzymatic Methods.- 1.7.3. Location of Disulfide Bridges.- 1.7.4. Mass Spectrometry Applied to Amino-Acid-Sequence Determination.- 1.8. Reagents Specific for Particular Amino Acids in Proteins.- 1.8.1. Amino Groups.- 1.8.2. Tyrosine.- 1.8.3. Carboxyl Groups.- 1.9. References.- 2 The Chemistry and Reactivity of Silk.- 2.1. Introduction.- 2.2. Sources and Functions of Silk.- 2.3. Histology of Silk.- 2.4. Chemical Composition of Silk.- 2.5. Chemical Structure of Fibroin.- 2.5.1. Molecular-Weight Determination of Fibroin.- 2.5.2. N-Terminal Amino Acid Determination.- 2.5.3. Primary Structure of Fibroin as Determined by Acid Hydrolysis.- 2.5.4. Primary Structure of Fibroin as Determined by Enzymic Hydrolysis.- 2.5.4.1. Existence of Cystine in Silk Fibroin.- 2.6. Integrated Picture of the Fibroin Molecule.- 2.7. Studies on the Chemical Reactivity of Bombyx mori Silk Fibroin.- 2.7.1. Hydrolysis of Silk Fibroin.- 2.7.2. Chemical Modification of Silk by Alkalis.- 2.7.3. Oxidation and Induced Crosslinking of Silk Fibroin.- 2.8. Technological Processes Involved in Silk Dyeing and Finishing.- 2.8.1. Degumming of Silk.- 2.8.2. Bleaching of Silk.- 2.8.3. Weighting of Silk.- 2.8.4. Dyeing of Silk.- 2.8.5. Finishing of Silk.- 2.9. References.- 3 The Histology of Keratin Fibers.- 3.1. Introduction.- 3.2. Microscopy Methods.- 3.2.1. Optical Microscope Methods.- 3.2.2. Conventional Electron Microscope Methods.- 3.2.3. Scanning-Electron-Microscope Methods.- 3.3. The Hair Follicle.- 3.3.1. Genesis.- 3.3.2. Hair Growth Cycle.- 3.3.3. Structure of the Hair Follicle.- 3.3.3.1. Matrix.- 3.3.3.2. Melanocytes.- 3.3.3.3. Cortex.- 3.3.3.4. Cuticle.- 3.3.3.5. Medulla.- 3.3.3.6. Inner Root Sheath.- 3.3.3.7. Outer Root Sheath.- 3.3.4. Histochemistry.- 3.3.4.1. Cystine and Cysteine.- 3.3.4.2. Nucleic Acids.- 3.3.4.3. Carbohydrates.- 3.3.4.4. Lipids.- 3.3.4.5. Arginine and Citrulline.- 3.3.4.6. Enzymes.- 3.4. The Fully Keratinized Hair.- 3.4.1. General Structure.- 3.4.2. Surface Structure.- 3.4.3. Internal Structure.- 3.4.3.1. Cuticle.- 3.4.3.2. Epicuticle.- 3.4.3.3. Cortex.- 3.4.3.4. Medulla.- 3.4.3.5. Hair Pigment.- 3.4.4. Histochemistry.- 3.4.4.1. Cystine and Cysteine.- 3.4.4.2. Free Amino and Basic Groups.- 3.4.4.3. Carboxyl Groups.- 3.4.4.4. Tyrosine.- 3.5. References.- 4 The Chemical Composition and Structure of Wool.- 4.1. Introduction.- 4.2. Chemical Studies on Wool Proteins.- 4.2.1. Oxidized Wool Proteins-Keratoses.- 4.2.2. S-Carboxymethylated Wool Proteins.- 4.2.2.1. Low-Sulfur Proteins.- 4.2.2.2. High-Sulfur Proteins.- 4.2.3. Ultra-High-Sulfur Proteins.- 4.2.4. High-Glycine-Tyrosine Proteins.- 4.2.5. Histological Components of the Wool Fiber.- 4.2.6. Wool Root Proteins.- 4.3. Physical Studies.- 4.3.1. Physical Studies on Soluble Wool Protein Fractions.- 4.3.1.1. Molecular-Weight Studies.- 4.3.1.2. Optical Studies.- 4.3.2. X-Ray Studies on the Intact Fiber.- 4.4. An Integrated Picture of the Wool Fiber.- 4.5. Unsolved Problems and Future Trends.- 4.6. References.- 5 Chemical Reactions of Keratin Fibers.- 5.1. Introduction.- 5.2. Hydrolysis.- 5.2.1. Acid Hydrolysis.- 5.2.2. Alkaline Hydrolysis.- 5.2.3. Rupture of Disulfide Bonds and Formation of New Amino Acids.- 5.3. Reaction with Reducing Agents.- 5.3.1. Thiols.- 5.3.2. Phosphines.- 5.3.3. Sulfites.- 5.3.4. Bunte Salts (S-Alkyl Thiosulfates).- 5.3.5. Metal Hydrides.- 5.4. Reaction with Oxidizing Agents.- 5.4.1. Hydrogen Peroxide.- 5.4.2. Organic Peroxyacids.- 5.4.3. Inorganic Peroxoacids.- 5.4.3.1. Peroxodisulfate.- 5.4.3.2. Peroxomonosulfuric Acid (Caro's Acid).- 5.4.3.3. Perborate.- 5.4.3.4. Other Inorganic Peroxoacids.- 5.4.4. Permanganate.- 5.4.5. Periodic Acid.- 5.4.6. Chromium Compounds.- 5.4.7. Halogens and Derivatives.- 5.4.8. Partial Oxidation.- 5.5. Acylation.- 5.5.1. Carboxylic Acids and Anhydrides.- 5.5.2. Active Esters and Amides.- 5.5.3. Carboxylic Acid Chlorides.- 5.5.4. Cyanate, Isocyanates, and Isothiocyanates.- 5.5.5. Sulfonyl Halides.- 5.5.6. Lactones and Thiolactones.- 5.5.7. Dithiocarboxylic Acid Esters.- 5.6. Arylation.- 5.6.1. l-Fluoro-2,4-dinitrobenzene(FDNB).- 5.6.2. Cyanuric Halides and Derivatives.- 5.7. Alkylation.- 5.7.1. Alkyl Halides, ?-Haloacids, and Derivatives.- 5.7.2. Aziridines.- 5.7.3. Maleic Acid and Derivatives.- 5.7.4. Acrylonitrile.- 5.7.5. Vinyl Sulfones and Phosphonates.- 5.7.6. Vinylpyridines.- 5.7.7. Unsaturated Aldehydes.- 5.7.8. 1,4-Benzoquinone.- 5.7.9. N-Methylol Compounds.- 5.7.10. Esterification of Carboxyl Groups.- 5.7.10.1. Alcohols.- 5.7.10.2. Epoxides.- 5.7.10.3. Carbodiimides.- 5.8. Reaction with Electrophilic Reagents.- 5.8.1. Iodine.- 5.8.2. Tetranitromethane (TNM).- 5.8.3. Nitric Acid.- 5.8.4. Nitrous Acid.- 5.8.5. Diazonium Salts.- 5.9. Condensation with Carbonyl Reagents.- 5.9.1. Formaldehyde.- 5.9.2. Other Aldehydes.- 5.9.3. 1,2- and 1,3-Dicarbonyl Compounds.- 5.10. Reaction with Reactive Dyes.- 5.10.1. Nucleophilic Substitutions.- 5.10.2. Nucleophilic Additions.- 5.10.3. Hydrolysis of Reactive Dyes.- 5.10.4. Dyeing Human Hair with Reactive Dyes.- 5.11. References.- 6 Crosslinking and Self-Crosslinking in Keratin Fibers.- 6.1. Introduction.- 6.2. Naturally Occurring Crosslinks.- 6.2.1. Noncovalent Bonds.- 6.2.2. Covalent Bonds.- 6.3. Formation of Crosslinks without Incorporation of Artificial Bridge Residues.- 6.3.1. Self-Crosslinking Reactions Induced by the Action of Alkali, Hot Water Steam Dry Heat Amines.- 6.4. Formation of Crosslinks by Means of Artificial Bridge Residues.- 6.4.1. Bifunctional Reagents.- 6.4.1.1. Aryl Dihalides.- 6.4.1.2. Alkylene Halides.- 6.4.1.3. Aralkylene Halides.- 6.4.1.4. Acylating Reagents.- 6.4.1.5. Aldehydes.- 6.4.1.6. Diisocyanates.- 6.4.1.7. Dimaleimides.- 6.4.1.8. Benzoquinone.- 6.4.1.9. bis-Diazohexane.- 6.4.1.10. Divinylsulfone.- 6.4.2. Reaction of Reactive Dyes with Wool.- 6.5. Analysis and Methods for Studying Crosslinking Reactions.- 6.5.1. Solubility Tests.- 6.5.2. Separation Procedures.- 6.5.3. Estimation of Reacted and Unreacted Side-Chain Groups.- 6.5.4. Isolation of Crosslinked Amino Acid Residues.- 6.6. Relationship between Morphological Fractions and Crosslinking Activity.- 6.7. Concluding Remarks.- 6.8. References.- 7 The Dyeing of Wool.- 7.1. Introduction.- 7.2. Synthetic Dyes.- 7.3. Wool Fiber as a Substrate for Dyes.- 7.4. Acid Dyes.- 7.5. Metal-Complex Dyes.- 7.5.1. Structure of Metal-Dye Complexes.- 7.5.2. Acid-Dyeing Premetallized Dyes.- 7.5.3. Neutral-Dyeing Premetallized Dyes.- 7.6. Chrome Dyes.- 7.7. Reactive Dyes.- 7.8. Vat Dyes.- 7.9. Dyeing with Minimum Damage to the Fiber.- 7.10. References.- 8 The Chemistry of Wool Finishing.- 8.1. Introduction.- 8.2. Scouring.- 8.2.1. Fiber Lubricants.- 8.2.1.1. Water-Soluble Lubricants.- 8.2.1.2. Alkali-Soluble Lubricants.- 8.2.1.3. Solvent-Soluble Lubricants.- 8.2.2. Principles of Oil Removal.- 8.2.3. Factors Affecting the Results Obtained in Scouring.- 8.3. Setting Processes.- 8.3.1. General Theory of Setting.- 8.3.2. Setting of Chemically Modified Fibers.- 8.3.3. Setting in Various Media.- 8.3.4. Setting Processes.- 8.4. Milling and Felting.- 8.4.1. Causes of Felting.- 8.4.2. Conditions of Fulling.- 8.4.3. Methods of Preventing Felting.- 8.5. Mothproofing.- 8.5.1. Mothproofing Agents.- 8.6. Wool Bleaching.- 8.7. Durable-Press Finish for Wool.- 8.8. Wrinkle-Resistance.- 8.9. Oil- and Water-Repellency.- 8.10. Polymer Grafting.- 8.11. Carbonizing.- 8.12. References.- 9 Other Animal Fibers.- 9.1. Introduction.- 9.2. Hair Growth.- 9.3. Fibers as Keratins.- 9.3.1. X-Ray Diffraction Patterns and Crystallinity.- 9.3.2. Infrared Spectroscopy.- 9.3.3. Electron Spin Resonance.- 9.3.4. Differential Thermal Analysis.- 9.3.5. Ultraviolet Absorption Spectroscopy.- 9.3.6. Chemical Analyses.- 9.3.7. Kerateines.- 9.3.8. Keratoses.- 9.3.9. Abnormal Human Hairs.- 9.4. Inorganic Constituents.- 9.5. Morphology and Chemistry.- 9.5.1. Medullation.- 9.5.2. Types of Cortical Cell.- 9.5.3. Pigmentation.- 9.6. Effect of Chemical Reagents.- 9.6.1. Behavior during Processing.- 9.6.2. Tests for Damage.- 9.6.3. Supercontraction and Setting Behavior.- 9.6.4. Resin Impregnation and Sterilization.- 9.6.5. Egg Capsules.- 9.7. Effect of Bacteria and Enzymes.- 9.8. References.