Origins of Clinical Chemistry

PrefaceAcknowledgmentsIntroduction1. Protein: Concept and Controversy I. Protein: The Ubiquitous Molecule II. Metabolism of Protein III. The Development of Protein Chemistry IV. The Word and the Concept V. The Protein Theory of Mulder VI. Liebig's Analyses VII. Mulder's Conflict with Liebig VIII. Liebig's Laboratory at Giessen IX. Dumas2. The Colloidal State I. The Tyndall Effect II. The Ultramicroscope III. Different Worlds of Matter IV. The Size of Colloidal Particles3. The Origins of Organic Chemistry I. The Vital Force II. The Chemical Nature of Organic Compounds III. The Discovery of Oxygen, Nitrogen, and Hydrogen IV. Lavoisier V. The Diversity of Organic Compounds VI. Woehler's Synthesis of Urea VII. The New Organic Chemistry VIII. Discovery of the Amino Acids IX. Chemical Techniques for Separating Amino Acids X. The Vast Diversity of Protein Structure XI. Protein Structure: The Fischer-Hofmeister Theory XII. Molecular Size of Proteins4. The Kjeldahl Method for Nitrogen I. Introduction II. The Dumas Method for Nitrogen III. The Carlsberg Laboratory IV. Development of the Kjeldahl Method V. Impact of the Kjeldahl Method VI. Modifications and Improvements VII. Application of the Method to Combined Nitrogen VIII. Description of the Procedure IX. Current Status X. Kjeldahl Analysis of Plasma Proteins5. Classification of Proteins I. Introduction II. Simple Proteins III. Conjugated Proteins IV. Derived Proteins V. The Basis of Plasma Protein Analysis6. Detection of Protein I. Introduction II. Criteria of Purity III. Analysis of Protein7. Protein Fractionation I. Introduction II. Early Distinctions between Albumin and Globulin III. The Precipitating Action of Ammonium Sulfate IV. The Precipitating Action of Sodium Sulfate V. Howe's Method for Fractionating Serum Proteins VI. Advantages and Disadvantages of Howe's Method VII. Inhomogeneity of Salt-Precipitated Fractions VIII. Discrepancy between Electrophoresis and Salt Precipitation Methods IX. Modification and Improvement of Howe's Method X. Precipitation of Globulin with Sodium Sulfite XI. Protein Precipitation with Phosphate Buffers XII. Precipitating Action of Heavy Metals and Alkaloidal Reagents XIII. Precipitation with Organic Solvents8. Nonspecific Tests and Procedures I. Determination of Physical Properties of Protein Solutions II. The Turbidity Procedures9. Colorimetry and Photometry I. Introduction II. Colorimetry III. Nephelometry IV. Turbidimetry V. Photometric Colorimetry VI. The Biuret Reaction VII. Phenol Reaction for Tyrosine VIII. Ultraviolet Absorbance (250-300 nm) IX. Far Ultraviolet Absorbance (200-250 nm) X. Biuret: The Popular Choice XI. Albumin-Specific Dye Binding XII. Direct Colorimetric Analysis of Globulin XIII. Analysis of ?-Globulin XIV. Normal Serum Protein Values10. Svedberg and the Ultracentrifuge I. Introduction II. Early Work of Svedberg III. The Optical Centrifuge IV. Construction of the "Ultra-Centrifuge" V. Determining the Molecular Weight of Proteins VI. Physical Parameters Affecting the Analysis VII. The Oil-Turbine Ultracentrifuge VIII. Monodisperse Systems IX. Improvements in Design X. The Optical System XI. Later Designs of the Ultracentrifuge XII. The Existence of Proteins as Uniform Molecules XIII. Sedimentation Coefficient XIV. Limitation of Clinical Applications XV. Other Applications11. Tiselius and the Moving Boundary Electrophoresis I. Historical Introduction II. Early Experiments III. Modern Era of Protein Electrophoresis IV. Electrokinetic Phenomena of Protein Solutions V. Electrophoretic Techniques VI. A New Electrophoresis Instrument VII. The Moving Boundary Pattern VIII. Practical Disadvantages of Moving Boundary Electrophoresis IX. Nonclinical Applications X. Retrospect12. Zone Electrophoresis on Paper I. Historical Introduction II. Early Investigations with Support Media III. The Introduction of Paper Support for Protein Electrophoresis IV. Types of Apparatus V. Electrode Vessels VI. Characteristics of Electrophoresis on Support Media13. Quantitation on Paper with Protein Dye I. Introduction II. Dye Elution III. Optical Problems of Direct Scanning IV. Direct Scanning V. TheAnalytrol VI. The Empirical Nature of Protein Staining VII. Development of the Bromphenol Blue Staining Procedure VIII. The Versatility of Zone Electrophoresis IX. Quantitation and the Variability of Dye Uptake14. Other Stabilized Media for Zone Electrophoresis I. Cellulose Acetate Electrophoresis II. Agar Gel III. Agarose Gel IV. High-Resolution Electrophoresis V. Automation of Electrophoresis15. Immunochemistry of Proteins I. Principles II. Immunochemical Methods of Analysis III. Limitations of Immunological Methods IV. Instrumentation V. Early Clinical Applications VI. The Accelerating Effect of Hydrophilic Polymers VII. Discrete Sample Analysis16. Proteins in Urine I. Early History II. Original Observation of Bence Jones Protein III. Chemical Identity of Bence Jones Proteins IV. The Heat Test V. Electrophoretic Detection of the "M" Component VI. Transient Proteinuria VII. Renal Mechanism of Proteinuria VIII. Components of Urinary Proteins IX. Determination of Protein in Urine X. Technology of the Future17. Proteins in Cerebrospinal Fluid I. Discovery of Spinal Fluid II. Protein Content of Spinal Fluid III. Flocculation Tests IV. Quantitative Tests for Protein18. The Fibrinogen to Fibrin Transformation I. The Coagulation of Blood II. Fibrinogen Analysis III. Fibrinogen in Health and Disease19. Radioimmunoassay I. Radioimmunoassay II. Alternative Markers20. In SummationReferencesIndex