Peeters Protides of the Biological Fluids

Proceedings of the Twenty-Second Colloquium, Brugge, 1974
1. Auflage 2013
ISBN: 978-1-4831-8743-3
Verlag: Elsevier Science & Techn.
Format: PDF
Kopierschutz: 1 - PDF Watermark

E-Book, Englisch, 772 Seiten, Web PDF

Proteins and Related Subjects, Volume 22: Protides of Biological Fluids covers the proteins of the intercellular matrix, along with the genetic defects and polymorphism of the human plasma proteins and isotachophoresis. The text first deals with the connective tissue proteins, along with the anabolic and catabolic enzymes of connective tissues. Next, the selection details the isolation and purification of various proteins, their metabolism, and function. The text also talks about the genetic defects and polymorphism of human plasma proteins, which includes the abnormalities of specific proteins. The last section covers the utilization of isotachophoresis as an analytical tool for the detection and characterization of amino acids, low-weight metabolites, and proteins. The book will be of great use to students, researchers, and practitioners of biological science.

Autoren/Hrsg.

Peeters, H.

Inhaltsverzeichnis

1;Front Cover;1
2;Protides of the Biological Fluids;4
3;Copyright Page;5
4;Table of Contents;6
5;Preface;18
6;Acknowledgements;19
7;PART 1: THE THIRD ARNE TISELIUS MEMORIAL LECTURE;20
8;Chapter 1. Relation between Structure and Biologic Function of the Protease Inhibitors in the Extracellular Fluid;22
8.1;REFERENCES;31
9;SECTION A: Pro teins of the Intercellular Matrix;32
9.1;Chapter 2. Cellular Differentiation and the Morphogenesis of the Intercellular Matrix;34
9.1.1;ROLE OF THE ICM IN MORPHOGENESIS;36
9.1.2;ACKNOWLEDGEMENTS;39
9.1.3;REFERENCES;39
9.2;Chapter 3. The Role of Extracellular Matrix Macromolecules upon Cell Differentiation;42
9.2.1;INTRODUCTION;42
9.2.2;ISSUES RELATED TO CELL DIFFERENTIATION;42
9.2.3;THE EXTRACELLULAR MATRIX PHENOTYPE OF DIFFERENTIATING CELLS;43
9.2.4;EPITHELIAL-MESENCHYMAL INTERACTIONS DURING ODONTOGENESIS;45
9.2.5;REFERENCES;50
9.3;Chapter 4. Ultrastructural Study of the Fibroblastic Activities of Multipotent Cells in the Mollusc: Helix aspersaA;52
9.3.1;RESULTS AND DISCUSSION;52
9.3.2;CONCLUSIONS;58
9.3.3;REFERENCES;58
9.4;Chapter 5. Isolation and Culture Techniques of Fetal Calf Chondrocytes;60
9.4.1;MATERIAL AND METHODS;60
9.4.2;RESULTS AND DISCUSSION;61
9.4.3;CONCLUSIONS;64
9.4.4;ACKNOWLEDGEMENTS;64
9.4.5;REFERENCES;64
9.5;Chapter 6. Control of Ameloblasts Cytodifferentiation;66
9.5.1;1. INTRODUCTION;66
9.5.2;2. METHODS;66
9.5.3;3. RESULTS;66
9.5.4;4. DISCUSSION;68
9.5.5;REFERENCES;69
9.6;Chapter 7. Periaxial Extracellular Material and Vertebral Chondrogenesis;70
9.6.1;VERTEBRAL CHONDROGENESIS;70
9.6.2;THE PERIAXIAL EXTRACELLULAR MATERIAL;72
9.6.3;ROLE OF THE PERIAXIAL MATERIAL;72
9.6.4;CONCLUSIONS AND DISCUSSION;76
9.6.5;REFERENCES;77
9.7;Chapter 8. Collagen Resorption in Sponges: Involvement of Bacteria and Macrophages;78
9.7.1;MATERIAL AND METHODS;78
9.7.2;RESULTS;78
9.7.3;DISCUSSION;82
9.7.4;REFERENCES;82
9.8;Chapter 9. Calcite and Collagen in the Skeleton of the Cnidaria Veretillum cynomorium Pall. (Anthozoa. Pennatulidae);84
9.8.1;MATERIAL AND METHODS;84
9.8.2;RESULTS;86
9.8.3;DISCUSSION;88
9.8.4;ACKNOWLEDGEMENT;88
9.8.5;REFERENCES;88
9.9;Chapter 10. Influence of Some Purified Plasma Proteins on Collagen Synthesis in vitro;90
9.9.1;MATERIALS AND METHODS;90
9.9.2;RESULTS;92
9.9.3;DISCUSSION;93
9.9.4;ACKNOWLEDGEMENTS;93
9.9.5;REFERENCES;93
9.10;Chapter 11. In vitro Effects of D(—)penicillamine on Collagen Synthesisby Human Fibroblasts;94
9.10.1;REFERENCES;97
9.11;Chapter 12. Studies on Collagen in the Developing Arteries of the Chick;98
9.11.1;REFERENCES;101
9.12;Chapter 13. Post-translational Processing of Procollagen Polypeptides;102
9.12.1;REFERENCES;104
9.13;Chapter 14. The Function of Borohydride Reducible Componentsof Collagen;106
9.13.1;INTRODUCTION;106
9.13.2;CARTILAGE AND BONE COLLAGEN;106
9.13.3;ACKNOWLEDGEMENTS;109
9.13.4;REFERENCES;109
9.14;Chapter 15. Stability of Collagens from Articular Cartilage and from theHeart Valves of Pigs.Study of Collagen—Proteoglycan Interactions;110
9.14.1;MATERIALS AND METHODS;110
9.14.2;SHRINKAGE TEMPERATURE MEASUREMENT;110
9.14.3;DIFFERENTIAL THERMAL ANALYSIS (D.T.A.);111
9.14.4;X-RAY DIFFRACTION;111
9.14.5;PROTEOGLYCAN EXTRACTION;111
9.14.6;BIOCHEMICAL ANALYSIS;111
9.14.7;RESULTS;111
9.14.8;DISCUSSION;114
9.14.9;ACKNOWLEDGEMENTS;114
9.14.10;REFERENCES;114
9.15;Chapter 16. Confirmation and Additional Features of the Planar Waveform in Collagen Fibre;116
9.15.1;INTRODUCTION;116
9.15.2;REFERENCES;119
9.16;Chapter 17. Identification of Two Molecular Species of Collagen in Mammalian Intervertebral Disc;120
9.16.1;INTRODUCTION;120
9.16.2;MATERIALS AND METHODS;120
9.16.3;RESULTS;121
9.16.4;DISCUSSION;125
9.16.5;ACKNOWLEDGEMENTS;125
9.16.6;REFERENCES;125
9.17;Chapter 18. Collagen Crosslinking in Inflamed Tissues;126
9.17.1;REFERENCES;129
9.18;Chapter 19. Collagen and Proteoglycans Extraction from Normal and Osteo-arthritic Human Articular Cartilage;130
9.18.1;INTRODUCTION;130
9.18.2;MATERIALS;130
9.18.3;METHODS;130
9.18.4;RESULTS;131
9.18.5;DISCUSSION;133
9.18.6;ACKNOWLEDGEMENTS;134
9.18.7;REFERENCES;134
9.19;Chapter 20. Bone in Dermatosparaxis;136
9.19.1;REFERENCES;139
9.20;Chapter 21. Urinary Excretion of Hydroxylysyl Glycosides as anIndex of Collagen Metabolism in Disease;140
9.20.1;INTRODUCTION;140
9.20.2;MATERIAL AND METHODS;140
9.20.3;RESULTS;141
9.20.4;DISCUSSION;143
9.20.5;REFERENCES;144
9.21;Chapter 22. Non-polar Pep tide s from Elastin;146
9.21.1;INTRODUCTION;146
9.21.2;MATERIALS AND METHODS;146
9.21.3;RESULTS AND DISCUSSION;148
9.21.4;REFERENCES;154
9.22;Chapter 23. The Ultrastructural Organization of Elastin;156
9.22.1;SUMMARY;156
9.22.2;REFERENCES;163
9.23;Chapter 24. Isolation of Chemically Pure Elastins in a Form Suitable for Mechanical Testing;164
9.23.1;REFERENCES;167
9.24;Chapter 25. Electron Microscopical Studies on the Role of Microfibrils in Elastogenesis;168
9.24.1;MATERIALS AND METHODS;168
9.24.2;RESULTS;168
9.24.3;DISCUSSION;172
9.24.4;ACKNOWLEDGEMENT;174
9.24.5;REFERENCES;174
9.25;Chapter 26. Organ-Culture Studies on the Biosynthesis of Intercellular Macromolecules of Aorta;176
9.25.1;MATERIAL AND METHODS;176
9.25.2;RESULTS AND DISCUSSION;176
9.25.3;CONCLUSIONS;178
9.25.4;ACKNOWLEDGEMENTS;178
9.25.5;REFERENCES;178
9.26;Chapter 27. Isolation and Characterization of a Highly Cross-linked Peptide of Elastin from Porcine A orta;180
9.26.1;INTRODUCTION;180
9.26.2;MATERIALS AND METHODS;180
9.26.3;RESULTS AND DISCUSSION;182
9.26.4;REFERENCES;183
9.27;Chapter 28. Characterization of Lipid Classes associated with ElastinIsolated from Normal and Pathological Human Aorta;186
9.27.1;INTRODUCTION;186
9.27.2;MATERIALS AND METHODS;186
9.27.3;RESULTS AND DISCUSSION;186
9.27.4;CONCLUSIONS;188
9.27.5;REFERENCES;189
9.28;Chapter 29. Structure and Aggregation of Proteoglycans of Cartilage;190
9.28.1;METHODS;190
9.28.2;RESULTS AND DISCUSSION;190
9.28.3;CONCLUSION;195
9.28.4;ACKNOWLEDGEMENTS;195
9.28.5;REFERENCES;195
9.29;Chapter 30. Structure of Cartilage Proteoglycans and Their Interaction with Some Intercellular Matrix Components;196
9.29.1;METHODS;196
9.29.2;RESULTS AND DISCUSSION;196
9.29.3;CONCLUSIONS;201
9.29.4;ACKNOWLEDGEMENTS;201
9.29.5;REFERENCES;201
9.30;Chapter 31. Structure of L-iduronic Acid-Sulphate-containing Oligosaccharides from Pig Skin Dermatan Sulphate;202
9.30.1;MATERIALS;202
9.30.2;METHODS;202
9.30.3;DISCUSSION;209
9.30.4;ACKNOWLEDGEMENTS;210
9.30.5;REFERENCES;210
9.31;Chapter 32. Chemical and Electron Microscopic Studies on Proteoglycans of Guinea Pig Costal Cartilage;212
9.31.1;CHEMICAL STUDIES;212
9.31.2;ELECTRON MICROSCOPIC STUDIES;213
9.31.3;CONCLUSIONS;217
9.31.4;ACKNOWLEDGEMENTS;218
9.31.5;REFERENCES;218
9.32;Chapter 33. Gel Electrophoresis of Proteoglycans and Collagen from Normal and Abnormal Growth Cartilage;220
9.32.1;METHODS;220
9.32.2;MATERIAL STUDIED;220
9.32.3;RESULTS AND DISCUSSION;221
9.32.4;ACKNOWLEDGEMENTS;223
9.32.5;REFERENCES;223
9.33;Chapter 34. The Control of the Early Steps in Polysaccharide Synthesis;224
9.33.1;THE PYROPHOSPHORYLASE REACTION;224
9.33.2;PYROPHOSPHORYLASES IN OTHER TISSUES;226
9.33.3;THE SIGNIFICANCE OF PYROPHOSPHORYLYSIS REACTIONS;228
9.33.4;CONTROL OF THE EARLY STEPS OF SUGAR NUCLEOTIDE METABOLISM;229
9.33.5;ACKNOWLEDGEMENT;229
9.33.6;REFERENCES;230
9.34;Chapter 35. UDP-Glucose: A Key Branch-point in the Regulation of Glycosaminoglycan Biosynthesis;232
9.34.1;ACKNOWLEDGEMENTS;235
9.34.2;REFERENCES;236
9.35;Chapter 36. Different Types of Chondroitin Sulfate-Dermatan Sulfate Hybrids in Arterial Tissue;238
9.35.1;1. METABOLIC HETEROGENEITY OF AORTIC HYALURONATE, HEPARAN SULFATE AND THE CHONDROITIN SULFATE/DERMATAN SULFATE FRACTION;238
9.35.2;2. 14C-LABELLED CS-DS SUBFRACTIONS;239
9.35.3;3. METABOLIC HETEROGENEITY OF DIFFERENT CS-DS HYBRIDS;241
9.35.4;CONCLUDING REMARKS;244
9.35.5;REFERENCES;245
9.36;Chapter 37. Incorporation of N-acetyl-D(l14 C)-Glucosamine in the Cartilage of a Selacian, Scyliorhinus canicula;246
9.36.1;ACTIVITY OF THE ENZYMES INVOLVED IN THE METABOLISM OF N-ACETYLGLUCOSAMINE;246
9.36.2;INCORPORATION OF N-ACETYL-D(I14C)-GLUCOSAMINE INTO THE GLYCOSAMINOGLYCANS;247
9.36.3;REFERENCES;250
9.37;Chapter 38. Biosynthesis of Acid Mucopolysaccharides by the Surviving Newborn Rat Skin;252
9.37.1;REFERENCES;256
9.38;Chapter 39. Biosynthesis of Chondroitin Sulfate Proteins. Isolation of an Insoluble Priming Pool Feeding One Collagen-bound and Three Soluble Pools with Heterogeneous Proteoglycans;258
9.38.1;I. EXPERIMENTAL TECHNIQUES;258
9.38.2;II. RESULTS AND DISCUSSION;259
9.38.3;ACKNOWLEDGEMENTS;261
9.38.4;REFERENCES;261
9.39;Chapter 40. The Variations of Bovine Cartilage Proteoglycans with Age;264
9.39.1;INTRODUCTION;264
9.39.2;MATERIALS AND METHODS;264
9.39.3;RESULTS AND DISCUSSION;265
9.39.4;REFERENCES;268
9.39.5;ACKNOWLEDGEMENTS;268
9.40;Chapter 41. Distribution and Biosynthesis of Glycosaminoglycans in Arterial Wall;270
9.40.1;REFERENCES;273
9.41;Chapter 42. Acid Mucopolysaccharides in Normal and Atherosclerotic Tissues: A Comparative Study;274
9.41.1;INTRODUCTION;274
9.41.2;MATERIAL AND METHODS;274
9.41.3;RESULTS AND DISCUSSION;274
9.41.4;REFERENCES;276
9.42;Chapter 43. Analysis of Urinary Mucopolysaccharides from Mucopolysaccharidose Cases by Gas-Liquid Chromatography;278
9.42.1;REFERENCES;281
9.43;Chapter 44. Sulfatase Deficiencies in Mucopolysaccharidoses;282
9.43.1;1. DIAGNOSIS OF SANFILIPPO A DISEASE FROM LEUKOCYTES AND CULTURED AMNIOTIC FLUID CELLS;282
9.43.2;2. DEFICIENCY OF SULFOIDURONIDE SULFATASE AND HEPARAN SULFATE SULFAMIDASE IN MUCOSULFATIDOSIS FIBROBLASTS;284
9.43.3;3. DEFICIENCY OF A SULFATASE ASSOCIATED WITH MAROTEAUX-LAMY'S DISEASE;284
9.43.4;ACKNOWLEDGEMENTS;285
9.43.5;REFERENCES;285
9.44;Chapter 45. The Proteoglycans of Articular Cartilage in Early Experimental Osteoarthrosis;288
9.44.1;METHODS;288
9.44.2;DISSECTION OF CARTILAGE;288
9.44.3;EXTRACTION OF PROTEOGLYCANS;289
9.44.4;RESULTS;289
9.44.5;DISCUSSION;292
9.44.6;REFERENCES;293
9.45;Chapter 46. Specificity of Pinocytosis of a-N-acetylglucosaminidase by Fibroblasts;294
9.45.1;ACKNOWLEDGEMENT;297
9.45.2;REFERENCES;297
9.46;Chapter 47. The Effect of O-ß-hydroxyaethylrutoside and (+)-catechine on Sulfate Incorporation of Fibroblasts inTissue Culture;298
9.46.1;INTRODUCTION;298
9.46.2;RESULTS;298
9.46.3;SUMMARY;300
9.46.4;ACKNOWLEDGEMENTS;301
9.46.5;ADDENDUM;301
9.46.6;REFERENCES;301
9.47;Chapter 48. Isolation and Primary Characterization of a Non-collagenous Reticulin Component;302
9.47.1;MATERIAL AND METHODS;302
9.47.2;RESULTS;303
9.47.3;REFERENCES;304
9.48;Chapter 49. The Isolation and Characterization of Non-Collagenous Proteins from the Intercellular Matrix;306
9.48.1;REFERENCES;308
9.49;Chapter 50. Isolation and Structural Study of Glycoproteins associated with Rabbit and Rat Dermis Collagen;310
9.49.1;EXPERIMENTAL METHODS;310
9.49.2;RESULTS;310
9.49.3;DISCUSSION;314
9.49.4;ACKNOWLEDGEMENTS;315
9.49.5;REFERENCES;315
9.50;Chapter 51. Structural Glycoproteins from Connective Tissues;316
9.50.1;MATERIAL AND METHODS;316
9.50.2;RESULTS AND DISCUSSION;318
9.50.3;ACKNOWLEDGEMENTS;320
9.50.4;REFERENCES;320
9.51;Chapter 52. An Immunohistological Study of the Distribution of Immunoglobulins, Collagen and Contractile Proteins inHuman Placentae;322
9.51.1;ACKNOWLEDGEMENTS;326
9.51.2;REFERENCES;326
9.52;Chapter 53. Human Serum Low Density Lipoglycoproteins: Carbohydrate Composition in Health and Disease;328
9.52.1;INTRODUCTION;328
9.52.2;MATERIALS AND METHODS;328
9.52.3;RESULTS AND DISCUSSION;329
9.52.4;ACKNOWLEDGEMENTS;332
9.52.5;REFERENCES;332
9.53;Chapter 54. Interaction between Plasma Proteins and the Intercellular Matrix in Human Aortic Intima;334
9.53.1;METHODS;334
9.53.2;RESULTS AND DISCUSSION;335
9.53.3;CONCLUSIONS;337
9.53.4;ACKNOWLEDGEMENTS;337
9.53.5;REFERENCES;337
9.54;Chapter 55. Thermoanalytical Studies on the Intercellular Matrix of theVessel Wall;338
9.54.1;REFERENCES;341
9.55;Chapter 56. Studies on the Regulation of the Biosynthesis of the Intercellular Macromolecules of the Corneal Stroma;342
9.55.1;MATERIALS AND METHODS;342
9.55.2;RESULTS;343
9.55.3;CONCLUSIONS;345
9.55.4;ACKNOWLEDGEMENTS;345
9.55.5;REFERENCES;345
9.56;Chapter 57. Water — Soluble Proteins from Egg-Shell Matrices;346
9.56.1;1. INTRODUCTION;346
9.56.2;2. EXPERIMENTAL;346
9.56.3;3. RESULTS AND DISCUSSION;346
9.56.4;4. SUMMARY;349
9.56.5;ACKNOWLEDGEMENT;350
9.56.6;REFERENCES;350
9.57;Chapter 58. Pseudomyxomatous Mucin: Characterization of a Non-compatible A Blood Group Activity in the Products of Pronase Digestion;352
9.57.1;INTRODUCTION;352
9.57.2;MATERIAL AND METHODS;352
9.57.3;RESULTS AND DISCUSSION;353
9.57.4;REFERENCES;354
9.58;Chapter 59. Isolation and Characterization of Structural Glycoproteins from Sponges;356
9.58.1;MATERIALS AND METHODS;356
9.58.2;RESULTS;357
9.58.3;CONCLUSIONS;360
9.58.4;REFERENCES;360
9.59;Chapter 60. Functional Role of the Macromolecules of the Intercellular Matrix in the Blood—Brain Barrier;362
9.59.1;CONCLUSIONS;366
9.59.2;ACKNOWLEDGEMENTS;366
9.59.3;REFERENCES;367
9.60;Chapter 61. Selective Cleavage of Basement Membrane Proteins at the Carboxyl Peptide Linkages of Methionine and at the Amino Peptide Linkages of Cysteine Residues;368
9.60.1;INTRODUCTION;368
9.60.2;RESULTS AND DISCUSSION;369
9.60.3;ACKNOWLEDGEMENTS;375
9.60.4;REFERENCES;375
9.61;Chapter 62. Basement Membrane Synthesis, Accumulation and Turnover in vitro;376
9.61.1;ACCUMULATION OF BASEMENT MEMBRANE;376
9.61.2;IDENTIFICATION OF CELLS SYNTHESIZING BASEMENT MEMBRANE COLLAGEN;377
9.61.3;RATES OF SYNTHESIS AND TURNOVER OF BASEMENT MEMBRANE COLLAGEN;378
9.61.4;EFFECTS OF LATHYROGENS ON SOLUBILITY OF NEW BASEMENT MEMBRANECOLLAGEN;380
9.61.5;CONCLUSIONS;380
9.61.6;ACKNOWLEDGEMENTS;380
9.61.7;REFERENCES;380
9.62;Chapter 63. An Intercellular Component of the Nervous System;382
9.62.1;INTRODUCTION;382
9.62.2;MATERIAL AND METHODS;382
9.62.3;RESULTS;383
9.62.4;CONCLUSION;385
9.62.5;REFERENCES;385
9.63;Chapter 64. Primary Structure of Glycopeptide Antigenic Site Isolated from Glomerular Basement Membrane;386
9.63.1;INTRODUCTION;386
9.63.2;MATERIAL;386
9.63.3;METHODS;386
9.63.4;RESULTS;387
9.63.5;CONCLUSIONS;390
9.63.6;REFERENCES;390
9.64;Chapter 65. Possible Mechanisms of Collagen Breakdown in Higher Animals;392
9.64.1;INTRODUCTION;392
9.64.2;REFERENCES;396
9.65;Chapter 66. Collagenases from Lower Organisms;398
9.65.1;SUMMARY;398
9.65.2;REFERENCES;407
9.66;Chapter 67. The Precursor of Bone Collagenase and its Activation;410
9.66.1;COLLAGENASE AND PROCOLLAGENASE;410
9.66.2;ACTIVATION OF PROCOLLAGENASE BY LYSOSOMES (CATHEPSIN Bx), KALLIKREINAND PLASMIN;410
9.66.3;INVOLVEMENT OF A "PROACTIVATOR-ACTIVATOR" ENZYME SYSTEM IN THEACTIVATION OF PROCOLLAGENASE;411
9.66.4;THE SIGNIFICANCE OF PROCOLLAGENASE AND OF ITS ACTIVATING SYSTEM;414
9.66.5;ACKNOWLEDGEMENTS;415
9.66.6;REFERENCES;415
9.67;Chapter 68. Existence of a Collagen Synthetase in the Microsomal Membranes of Rat Liver;418
9.67.1;MATERIAL AND METHODS;418
9.67.2;RESULTS;419
9.67.3;DISCUSSION;422
9.67.4;ACKNOWLEDGEMENT;422
9.67.5;REFERENCES;422
9.68;Chapter 69. Collagenolytic Enzymes in Invasion Zones of Tumours;424
9.68.1;REFERENCES;426
9.69;Chapter 70. Induction of Collagenolytic Enzymes and Catalase in Ascites Cells Growing as Solid Invasive Tumour;428
9.69.1;REFERENCES;431
9.70;Chapter 71. Aortic Elastase, Its Role in the Degradation of A rterial Elas tin;432
9.70.1;MATERIALS AND METHODS;432
9.70.2;RESULTS;433
9.70.3;CONCLUSIONS;436
9.70.4;ACKNOWLEDGEMENTS;436
9.70.5;REFERENCES;436
9.71;Chapter 72. Purification and Characterization of Human Blood Platelet Elastase;438
9.71.1;PURIFICATION OF THE TRYPSIN INDEPENDENT ELASTASE;438
9.71.2;PURIFICATION OF THE TRYPSIN-DEPENDENT ELASTASE FROM THE "FIXATION PEAKS";440
9.71.3;ELECTROPHORESIS STUDIES OF THE TRYPSIN-DEPENDENT ANDTRYPSIN-INDEPENDENT ELASTASES;440
9.71.4;ABBREVIATIONS;442
9.71.5;ACKNOWLEDGEMENT;442
9.71.6;REFERENCES;443
9.72;Chapter 73. Change of Serie Inhibiting Power against Elastase in Experimental A therosclerosis;444
9.72.1;INTRODUCTION;444
9.72.2;EXPERIMENTAL;444
9.72.3;RESULTS;446
9.72.4;DISCUSSION - CONCLUSION^6"8);448
9.72.5;REFERENCES;449
9.73;Chapter 74. Degradation of Chondroitin Sulphate by Lysosomal Enzymes from Embryonic Chick Cartilage;450
9.73.1;INTRODUCTION;450
9.73.2;RESULTS AND DISCUSSION;450
9.73.3;ACKNOWLEDGEMENTS;454
9.73.4;REFERENCES;454
9.74;Chapter 75. The Possible Function of Lysozyme in Cartilage Metabolism;456
9.74.1;ACKNOWLEDGEMENTS;459
9.74.2;REFERENCES;459
9.75;Chapter 76. Specificity Requirements of Lysyl Oxidase;460
9.75.1;REFERENCES;462
10;SECTION B: Genetic Defects and Polymorphism of Human Plasma Proteins;464
10.1;Chapter 77. Biological and Medical Aspects of Inherited Protein Polymorphism;466
10.1.1;REFERENCES;471
10.2;Chapter 78. Regulation of Plasma Protein Synthesis in Cultured Embryonic Chick-liver Cells:Lack of Translational Control;472
10.2.1;SUMMARY;472
10.2.2;INTRODUCTION;472
10.2.3;MATERIALS AND METHODS;472
10.2.4;RESULTS AND DISCUSSION;473
10.2.5;CONCLUSION;476
10.2.6;REFERENCES;476
10.3;Chapter 79. Post-synthetic Isomerization of Rabbit Serum Albumin;478
10.3.1;REFERENCES;482
10.4;Chapter 80. Plasma Albumin Polymorphism in Fowl.A System for the Study ofAlbumin Biosynthesis and Its Control;484
10.4.1;REFERENCES;489
10.5;Chapter 81. A nalbuminaemia;490
10.5.1;REFERENCES;493
10.6;Chapter 82. Alloalbumin B and its Subtypes;494
10.6.1;REFERENCES;495
10.7;Chapter 83. The Differential Binding of Bromophenol Blue studied insix new Propositi with Bisalbuminaemia of theAI Ge Type;496
10.7.1;ABSTRACT;496
10.7.2;REPORT;496
10.7.3;CONCLUSIONS;499
10.7.4;REFERENCES;499
10.8;Chapter 84. Simultaneous Turnover Studies of theTwo Albumin Components Alternatively Labelled with1251 and 131I in Human Bisalbuminaemia;500
10.8.1;INTRODUCTION;500
10.8.2;MATERIALS AND METHODS;500
10.8.3;RESULTS AND DISCUSSION;503
10.8.4;CONCLUSIONS;503
10.8.5;REFERENCES;506
10.9;Chapter 85. The Pi System: Polymorphism of Alpha-1-Antitrypsin;508
10.9.1;REFERENCES;511
10.10;Chapter 86. Pi Typing Techniques;512
10.10.1;REFERENCES;514
10.11;Chapter 87. Antitryptic Activity of Alpha j-anti try psin Pi Bands in Starch Gel;516
10.11.1;MATERIALS AND METHODS;516
10.11.2;RESULTS;516
10.11.3;DISCUSSION;517
10.11.4;REFERENCES;518
10.12;Chapter 88. a ^Antitrypsin Deficiency: Pi Genotype ZO, SO and MO;520
10.12.1;MATERIAL AND METHODS;520
10.12.2;FAMILY HISTORY;520
10.12.3;RESULTS;520
10.12.4;DISCUSSION;521
10.12.5;ACKNOWLEDGEMENT;522
10.12.6;REFERENCES;522
10.13;Chapter 89. Structural Differences Between Pi-Types of a1-antitrypsin;524
10.13.1;MATERIAL AND METHODS;524
10.13.2;RESULTS AND DISCUSSION;525
10.13.3;ACKNOWLEDGEMENT;528
10.13.4;REFERENCES;528
10.14;Chapter 90. Chemical Properties of a1 -antitrypsin;530
10.14.1;INTRODUCTION;530
10.14.2;RESULTS AND DISCUSSION;530
10.14.3;DESCRIPTION OF THE METHOD;530
10.14.4;ACKNOWLEDGEMENTS;533
10.14.5;REFERENCES;533
10.15;Chapter 91. The Pi System: Its Study by means of Thin-Layer-Gel Electrofocusing in Poly aery lamide Gel;534
10.15.1;SUMMARY;534
10.15.2;INTRODUCTION;534
10.15.3;MATERIALS AND METHODS;534
10.15.4;RESULTS;535
10.15.5;DISCUSSION;537
10.15.6;ACKNOWLEDGEMENTS;539
10.15.7;REFERENCES;539
10.16;Chapter 92. a1 -Antitrypsin (Pi) Phenotypes in Neonatal Liver Disease;540
10.16.1;HISTOLOGICAL EXAMINATION;540
10.16.2;FAMILY STUDIES;541
10.16.3;COMMENT;541
10.16.4;REFERENCES;544
10.17;Chapter 93. Genetic Complement Defects in Man;546
10.17.1;REFERENCES;552
10.18;Chapter 94. The Role of Complement in Immune Hemolysisin vitro and in vivo;554
10.18.1;REFERENCES;559
10.19;Chapter 95. Hidden C3-Variants and Diverse Phenotypes of Unconverted and Converted C3;560
10.19.1;SUMMARY;560
10.19.2;ACKNOWLEDGEMENTS;565
10.19.3;REFERENCES;565
10.20;Chapter 96. The Metabolism of Radiolabelled C3 f1251-C3) in Autoimmune Disorders;566
10.20.1;REFERENCES;569
10.21;Chapter 97. Critical Factors for the Immuno chemical Quantitation of theThird Complement Component C3;570
10.21.1;MATERIALS AND METHODS;570
10.21.2;RESULTS;571
10.21.3;DISCUSSION;571
10.21.4;REFERENCES;573
10.22;Chapter 98. A New Type of Very Slow C3;574
10.22.1;ABSTRACT;574
10.22.2;INTRODUCTION;574
10.22.3;METHODS;574
10.22.4;RESULTS;575
10.22.5;DISCUSSION;577
10.22.6;REFERENCES;577
10.23;Chapter 99. The Frequency of the Polymorphisms of C3 in the Swiss Population and Some Remarks on the Identification of Rare Phenotypes;578
10.23.1;REFERENCES;581
10.24;Chapter 100. Sources of error in C3-typing by High-voltage Agarose Gel Electrophoresis;582
10.24.1;REFERENCES;584
10.25;Chapter 101. C2 Deficiency in Man;586
10.25.1;INTRODUCTION;586
10.25.2;BIOCHEMICAL NATURE OF THE DEFECT;587
10.25.3;IN VITRO STUDIES OF COMPLEMENT MEDIATED FUNCTION;587
10.25.4;IN VIVO STUDIES OF COMPLEMENT MEDIATED FUNCTIONS;590
10.25.5;COMMENTS;591
10.25.6;CONCLUSIONS;592
10.25.7;ACKNOWLEDGEMENTS;593
10.25.8;REFERENCES;593
10.26;Chapter 102. Polymorphism of Human C6;594
10.26.1;INTRODUCTION;594
10.26.2;METHODS AND MATERIALS;594
10.26.3;DISCUSSION;598
10.26.4;ACKNOWLEDGEMENTS;599
10.26.5;REFERENCES;599
10.27;Chapter 103. Cl Deficiency in Man;600
10.27.1;REFERENCES;602
10.28;Chapter 104. A Modified Technique in Typing Pt Proteins;604
10.28.1;REFERENCES;607
10.29;Chapter 105. Structural Characterization and Genetic Variation of Haptoglobin;608
10.29.1;HAPTOGLOBIN POLYMORPHISM;608
10.29.2;RARE GENETIC VARIANTS OF HAPTOGLOBIN;611
10.29.3;POLYMER FORMATION OF HAPTOGLOBIN;612
10.29.4;HAPTOGLOBIN FROM SPECIES OTHER THAN HUMAN;613
10.29.5;HAPTOGLOBIN BETA CHAIN;613
10.29.6;ACKNOWLEDGEMENTS;614
10.29.7;REFERENCES;614
10.30;Chapter 106. Comparison of the Primary Structure of the ß-Chain of Haptoglobin with Serine Proteases;616
10.30.1;METHODS;616
10.30.2;RESULTS AND DISCUSSION;618
10.30.3;ACKNOWLEDGEMENT;620
10.30.4;REFERENCES;621
10.31;Chapter 107. Structural Aspects of Haemoglobin/Haptoglobin Interaction;622
10.31.1;INTRODUCTION;622
10.31.2;MATERIALS AND METHODS;622
10.31.3;RESULTS AND DISCUSSION;622
10.31.4;ACKNOWLEDGEMENTS;625
10.31.5;REFERENCES;625
10.32;Chapter 108. Formation of Haptoglobin—Haemoglobin Complex inInactivated Sera;626
10.32.1;SUMMARY;626
10.32.2;REFERENCE;629
10.33;Chapter 109. Close Linkage Between LCAT (Lecithin: Cholesterol Acyltransferase) Locus and a-Haptoglobin Locus on Chromosome No. 16;630
10.33.1;INTRODUCTION;630
10.33.2;MATERIALS AND METHODS;630
10.33.3;RESULTS AND DISCUSSION;631
10.33.4;REFERENCES;633
10.34;Chapter 110. Genetic Variations in Serum Lipoproteins;634
10.34.1;CATEGORIES OF LIPOPROTEIN VARIATION OBSERVABLE IN MAN;634
10.34.2;NORMAL GENETIC VARIATION IN SERUM LIPOPROTEINS;635
10.34.3;NORMAL LIPOPROTEIN VARIATION IN ANIMALS;637
10.34.4;INHERITED LIPOPROTEIN ANTIGENS AND DISEASE;637
10.34.5;CONCLUDING REMARKS;638
10.34.6;REFERENCES;639
10.35;Chapter 111. Computer Model of Lipoprotein Metabolism in Hyperlipopro tein em ia;640
10.35.1;REFERENCES;644
10.36;Chapter 112. Recent Progress in the Investigation of the Ag-System of Betalipoproteins;646
10.36.1;THE NEW FACTOR Ag(i);646
10.36.2;PRESENT GENETIC CONCEPT OF THE Ag(a1 ,c,d,g,h,i,t,x,y,z) SYSTEM;648
10.36.3;REFERENCES;651
10.37;Chapter 113. The Relation of Artefactual and Real Polymorphism of Human Ceruloplasmin to its Polypeptide Chain and Carbohydrate Structure;652
10.37.1;SUBUNIT HETEROGENEITY AND ITS RELATION TO PROTEOLYTICFRAGMENTATION;652
10.37.2;CARBOHYDRATE STRUCTURE AND HETEROGENEITY;655
10.37.3;THE CERULOPLASMIN MAJOR AND MINOR FORM AND CARBOHYDRATESTRUCTURE;655
10.37.4;ACKNOWLEDGEMENT;658
10.37.5;REFERENCES;658
10.38;Chapter 114. Various Types of Congenital Fibrinogen Defects;660
10.38.1;REFERENCES;662
10.39;Chapter 115. Urinary Fibrin Split Products in Experimental and Human Glomerulonephritis;664
10.39.1;METHODS, MATERIAL AND PATIENTS;664
10.39.2;RESULTS;665
10.39.3;DISCUSSION;667
10.39.4;REFERENCES;667
10.40;Chapter 116. Association of Typhoid Fever and Response to Vaccination with Polymorphic Systems in Man;668
10.40.1;ACKNOWLEDGEMENTS;672
10.40.2;REFERENCES;672
10.41;Chapter 117. On the Occurrence of a Genetically Determined "Third" Beta-Globulin;674
10.41.1;INTRODUCTION;674
10.41.2;GENETIC STUDY;674
10.41.3;NATURE OF THIS GLOBULIN;674
10.41.4;CONCLUSIONS;677
10.41.5;ACKNOWLEDGEMENTS;677
10.41.6;REFERENCES;677
11;SECTION C: Isotachophoresis;678
11.1;Chapter 118. Analytical Isotachophoresis—Principles of Separation and Detection;680
11.1.1;INTRODUCTION;680
11.1.2;SEPARATION PRINCIPLE;680
11.1.3;DETECTION PRINCIPLES;682
11.1.4;INTERPRETATION OF DETECTOR SIGNALS;683
11.1.5;CONCLUSIONS;686
11.1.6;REFERENCES;686
11.2;Chapter 119. Free Displacement Electrophoresis (Isotachophoresis);688
11.2.1;SOME CHARACTERISTIC FEATURES OF THE METHOD;688
11.2.2;APPLICATIONS;688
11.2.3;ACKNOWLEDGEMENTS;691
11.2.4;REFERENCES;691
11.3;Chapter 120. Potential Use of Isotachophoresis in Space;692
11.3.1;INTRODUCTION;692
11.3.2;SPACE EXPERIMENTS;692
11.3.3;ISOTACHOPHORESIS;693
11.3.4;CONCLUSIONS;697
11.3.5;REFERENCES;697
11.4;Chapter 121. Preparative Isotachophoresis of Membrane Proteins in Solubilizing and Dissociating Media;698
11.4.1;ERYTHROCYTE MEMBRANE PROTEINS;698
11.4.2;MILK FAT GLOBULE MEMBRANE PROTEINS;700
11.4.3;BIOSPECIFIC INTERACTION IN ISOTACHOPHORESIS;700
11.4.4;ACKNOWLEDGEMENTS;702
11.4.5;NOTE;702
11.4.6;REFERENCES;702
11.5;Chapter 122. Preparative Isotachophoresis Combined with Biospecific Interaction and Neuraminidase Treatment in Purification of Human Serum Cholinesterase;704
11.5.1;INTRODUCTION;704
11.5.2;MATERIALS AND METHODS;704
11.5.3;RESULTS;705
11.5.4;DISCUSSION;708
11.5.5;ACKNOWLEDGEMENTS;708
11.5.6;REFERENCES;708
11.6;Chapter 123. Analytical Isotachophoresis in Capillary Tubes: Separation of Human Haemoglobin;710
11.6.1;INTRODUCTION;710
11.6.2;PRINCIPLE OF SEPARATION;710
11.6.3;RESULTS AND DISCUSSION;712
11.6.4;REFERENCES;714
11.7;Chapter 124. Isotachophoresis of Human Apo-HDL Polypeptides;716
11.7.1;EXPERIMENTAL;716
11.7.2;SAMPLE PREPARATION;716
11.7.3;RESULTS;717
11.7.4;CONCLUSION;719
11.7.5;REFERENCES;719
11.8;Chapter 125. The Application of Steady-State Stacking to Macromolecular Fractionation by Poly aery lamide Gel Electrophoresis;720
11.8.1;INTRODUCTION;720
11.8.2;METHODS;721
11.8.3;RESULTS;724
11.8.4;DISCUSSION;731
11.8.5;CONCLUSION;732
11.8.6;ACKNOWLEDGEMENTS;732
11.8.7;REFERENCES;732
11.9;Chapter 126. Purification Control of Synthetic Pep tides by Means of Analytical Isotachophoresis;734
11.9.1;INTRODUCTION;734
11.9.2;EXPERIMENTAL;734
11.9.3;RESULTS AND DISCUSSION;734
11.9.4;ACKNOWLEDGEMENT;738
11.9.5;REFERENCES;738
11.10;Chapter 127. Conductometric Detection During Isotachophoresis;740
11.10.1;INTRODUCTION;740
11.10.2;MATERIALS AND METHOD;740
11.10.3;EXPERIMENTAL CONDITIONS;745
11.10.4;ACKNOWLEDGEMENT;745
11.10.5;REFERENCES;745
11.11;Chapter 128. Isotachophoretic Studies of Adenosine Phosphates and Divalent Cations of Perfused Mouse Liver Cells;746
11.11.1;INTRODUCTION;746
11.11.2;MATERIALS AND METHODS;746
11.11.3;RESULTS;747
11.11.4;DISCUSSION;748
11.11.5;ACKNOWLEDGEMENTS;750
11.11.6;REFERENCES;750
11.12;Chapter 129. Isotachophoresis: A New Technique for Determination of Tissue Metabolite Concentrations;752
11.12.1;REFERENCES;755
11.13;Chapter 130. Analytical Isotachophoresis in capillary tubes: Preliminary study of Phenylketonuric Sera;756
11.13.1;INTRODUCTION;756
11.13.2;EXPERIMENTAL;757
11.13.3;RESULTS AND DISCUSSION;760
11.13.4;ACKNOWLEDGEMENT;761
11.13.5;REFERENCES;761
11.14;Chapter 131. Detection of Traces of Proteins by Isotachophoresis;762
11.14.1;INTRODUCTION;762
11.14.2;MATERIALS;762
11.14.3;METHODS;762
11.14.4;SAMPLES;763
11.14.5;RESULTS;763
11.14.6;CONCLUSION;766
11.14.7;ACKNOWLEDGEMENTS;766
11.14.8;REFERENCES;766
12;Author Index;768
13;Subject Index;770