Protides of the Biological Fluids

Protides of the Biological Fluids reviews trends in research concerning protides of the biological fluids, with emphasis on tumor-associated antigens (TAAs), lectins, and separation methods such as electrophoresis and isoelectric focusing. Examples of TAAs discussed in this book are carcinoembryonic antigens, mesenchyme-associated antigens, and oncofetal pancreatic antigens. The mode of action of lectins as well as lectin-binding sites are also considered.
This book is comprised of 195 chapters and begins with an overview of the strategy and monitoring of protein fractionation, followed by a discussion on the self-nonself concept of cancer and ""autoimmune"" diseases; presence of trophoblast antigens on the membranes of some human tumor and transformed cells; and non-specific cross-reacting antigens in human blood monocytes. Subsequent chapters explore the metabolism of carcinoembryonic antigen and alpha-fetoprotein during delivery; amino acid sequence identity of tissue polypeptide antigen fragments from different sources; isoferritins, glycoproteins, and viral antigens; and crossed immunoelectrophoresis of yeast plasma membrane lectin receptors. The final section is devoted to separation techniques such as isotachophoresis, chromatography, electrophoresis, and isoelectric focusing.
This monograph will be of value to biologists and researchers interested in protides of the biological fluids.

Contenu

Preface

Acknowledgments

The Eighth Arne Tiselius Memorial Lecture

Strategy and Monitoring of Protein Fractionation

Section A. Tumor Associated Antigens (TAA)

A.1. Introduction

Self-Nonself Concept of Cancer and 'Autoimmune' Diseases

A.2. Basic Data on TAA in Man

A.2.1. TA: Trophoblast Antigens

A.2.2. NCA: Non specific Cross Reacting Antigens

A.2.3. CEA: Carcino Embryonic Antigens

A.2.4. MAA: Mesenchyme Associated Antigens

A.2.5. AFP: Alfa Fetoproteins

A.2.6. OPA: Oncofetal Pancreatic Antigens

A.2.7. TPA: Tissue Polypeptide Antigens

A.2.8. Isoferritins

A.2.9. Glycoproteins

A.2.10. Viral Antigens

A.2.11. LAA: Leukemia Associated Antigens

A.3. Basic Data on TAA in Experimental Tumors

A.3.1. Hepatoma

A.3.2. Teratoma

A.3.3. Neuroblastoma

A.3.4. Mastocytoma

A.3.5. Leukemia

A.4. Tumor Markers as a Clinical Tool

A.4.1. Markers in Cancer Tissue

A.4.2. Markers in Plasma and Urine

Section B. Lectins

B.1. Characterization of Lee tins

Glycosyl Derivatives of Separon and their Use in Isolation and Immobilization of Lectins

Resedine: an Albumin-Inhibitable Lectin from Lawsonia inermis Var. "Reseda"

Some Properties of Rice Germ Agglutinin (RGA)

Characterization and Specificity of an Anti-N Lectin Isolated from Vioia graminea Seeds

Structure and Properties of the Toxic Lectin Modeccin

Pea Seed Lectin (PEA)

A Lectin from E. coli Specific for the Amino Acid L-Histidine

The Axinella Polypoides Lectins and their Occurrence in the Sponge Tissue

A Complement Activating Lectin from the Albumin Gland of Helix aspersa

Lymphocyte Agglutination and Hemagglutination Androctonus and Limulus Agglutinins

Lectins from the Horseshoe Crab, Limulus polyphemus3 Reactive with Bacterial Lipopolysaccharide

B.2. Mode of Action of Lectins

Control of Cell Aggregation by Membrane Macromolecules

The Interaction between Viruses and Lectins. The Contribution of Hydrophobic Bonding

A Study of Lectin Binding to Mammalian Lymphoid Cells Using Fluorochromasia and Fluorescence Polarization Techniques

Structure-Function Relationship among Leguminous Plant Lectins

Redistribution of Lentil Lectin Receptors on Rabbit Polymorphonuclear Membranes

Mechanism of the Interaction of Ricinus communis Lectins with Saccharides

Studies on the Specificities of Some Lectins

Anti-Glucuronyl Activity of Limulus polyphemus Agglutinin

B.3. Lectin Binding Sites

B.3.1. Binding Sites on Experimental Cells

B.3.2. Binding Sites on Human Cells

B.4. Lectin Binding to Cells

B.4.1. Erythrocytes

B.4.2. Lymphocytes

B.4.3. Other Cells

B.5. Lectins in Separation of Proteins

B.6· Clinical Applications of Lectins

Anti-Cancer Properties of the Toxic Lectins ABRIN and RICIN

Determination and Differentiation of Lectin - Glycoconjugate Interaction by Laser Nephelometry

A Nephelometric Assay of Concanavalin A Binding Proteins and its Use in Monitoring Inflammatory Disease

Lectin Characterization of Abnormal Cystic Fibrosis a-L-Fucosidase

Concanavalin A-Affinity Chromatography in the Diagnosis of Fetal Abnormalities

Staining of Carbohydrate Moiety of Fibrinogen and Factor VIII in Electrophoretic Gels with Fluorescein-Labeled Lectins

Section C. Techniques

C.1. Electrophoresis

Some Characteristic Reactions between Glycoproteins and Lectins in Analytical Affinity Electrophoresis

Sephadex Sandwich Disc Electrophoresis - Further Developments and Potential Applications

Molecular Weight Determination of Native Proteins by Electrophoresis in Linear Polyacrylamide Gradient Gels

Multifractionative Electrophoresis on Cellulose Acetate Wedge Shaped Strips. Identification of Protein Components

C.2. Isoelectric Focusing

Critical Parameters in Isoelectric Focusing

On the Determination of the Isoelectric Points of Proteins

The Chemical Properties of Pharmalyte

Isoelectric Focusing with PharmalyteTM in Gel Rods

The Use of 'Imphilytes' as Stationary Phases for Biospecific Elution Chromatography of Proteins

A Simple Method for Preparative Isoelectric Focusing in Thick Layers of Sephadex®

Agarose Isoelectric Focusing of Macroproteins

Titration Curves of Proteins by Two-Dimensional Isoelectric Focusing-Electrophoresis

Fingerprinting (Peptide Mapping) by Isoelectric Focusing

The Microheterogeneity and pI of Thyroxine-Binding Globulin Determined by Isoelectric Focusing on Cellulose Acetate and Agarose Followed by Immunofixation

C.3. Isotachophoresis

Column-Coupling in Electrophoresis

Isotachophoresis of Uremic Metabolites

C.4. Chromatography

C.4.1. Gels and Celluloses

C.4.2. Hydrophobie Gels

C.5. Affinity Chromatography

C.5.1. Basic Data

C.5.2. Affinity Applications

C.6. Isolation of Proteins

C.6.1. Plasma Proteins

C.6.2. Platelet Proteins

C.6.3. Placental Proteins

Author Index

Subject Index