Bibliographic Information

Isoenzymes

[by] J. Henry Wilkinson

(Science paperbacks, 112)

Chapman & Hall, 1975, c1970

2nd ed., pbk. ed

Available at  / 5 libraries

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Includes bibliographies

Description and Table of Contents

Description

The term isoenzyme is used to describe enzymically active proteins, catalysing the same reaction and occurring in the same species, but differing in certain of their physico-chemical properties. Although the occurrence of enzymes in multiple molecular forms has been recognized for several decades, the application of electrophoretic and, to a lesser extent, chromatographic techniques has led to rapid developments in recent years. Since the discovery of the heterogeneity of lactate dehy- drogenase, reported almost simultaneously by Vesel I and Beam and by Wieland and Pfleiderer in 1957, the multiple forms of this enzyme have become the subject of an extensive literature, and the techniques introduced have been applied to investigations of other isoenzymes. Isoenzymes, especially those of lactate dehydrogenase and alkaline phosphatase, have found many applications as diagnostic agents in clin- ical chemistry, while others, such as those of cholinesterase and glucose 6-phosphate dehydrogenase, exhibit a biological polymorphism of con- siderable interest in genetics. Recent additions to our understanding of the chemical structure of the lactate dehydrogenase isoenzymes have indicated their great potential in fields as diverse as immunology, em- bryology and comparative anatomy. These remarkable developments suggest that the time is opportune for present knowledge to be surveyed, and I have compiled this monograph in the hope that it will be found useful by biochemists, pathologists, clinicians, geneticists and others with interests in enzymology.

Table of Contents

  • 1 Introduction.- Nomenclature of multiple forms of enzymes. Numbering of isoenzymes.- 2 Techniques for the Separation of Isoenzymes.- Preparation of materials for isoenzyme separation. Electrophoretic techniques: general considerations
  • paper electrophoresis
  • starch-block electrophoresis
  • cellulose acetate electrophoresis
  • agar-gel electrophoresis
  • starch-gel electrophoresis
  • polyacrylamide-gel electrophoresis
  • column electrophoresis
  • iso-electric focusing. Chromatographic techniques:ion-exchange celluloses. Gel filtration.- 3 Detection and Determination of Isoenzymes.- Elution techniques: NAD- and NADP-dependent dehydrogenases
  • esterases
  • peroxidases. Detection of isoenzymes in electrophoretic media: 'enzymoelectrophoresis'
  • tetrazoliumstaining techniques
  • 'nothing dehydrogenase' effect
  • staining techniques for esterases.- 4 The Chemical Nature of Isoenzymes.- Sub-unit structure: lactate dehydrogenase
  • creatine kinase
  • aldolase
  • glucose 6-phosphate dehydrogenase
  • tryptophan synthetase
  • catalase
  • caeruloplasmin. Presence of charged groups in isoenzyme molecules: alkaline phosphatase. Polymerization as the source of enzyme heterogeneity: cholinesterases
  • amylase. Conformational isomerism: malate dehydrogenase. Differences in amino-acid sequence.- 5 Enzyme Multiplicity in the Glycolytic Pathway and the Pentose-Phosphate Cycle.- Hexokinase: detection of hexokinase after zone electrophoresis
  • hexokinase isoenzymes in the erythrocyte
  • hexokinase in other tissues. Phosphoglucomutase. Glucose 6-phosphate dehydrogenase: demonstration of glucose 6-phosphate dehydrogenase heterogeneity
  • chemical structure and properties of glucose 6-phosphate dehydrogenase
  • genetic variants of human erythrocytic glucose 6-phosphate dehydrogenase
  • glucose 6-phosphate dehydrogenase heterogeneity in other tissues. 6-Phosphogluconate dehydrogenase: heterogeneity in human erythrocytes
  • 6-phosphogluconate dehydrogenase isoenzymes in other species
  • structure of 6-phosphogluconate dehydrogenase isoenzymes. Phosphoglucose isomerase. Aldolase: classification of the aldolases
  • electrophoretic studies
  • fructose 1-phosphate aldolase. Glyceraldehyde 3-phosphate dehydrogenase. ?-Glycerophosphate dehydrogenase. Phosphopyruvate hydratase (enolase). Pyruvate kinase.- 6 Lactate Dehydrogenase Isoenzymes.- Distribution. Chemical and kinetic properties: substrate specificities and affinities
  • effect of pH variation
  • effects of inhibitors
  • reactions with coenzyme analogues
  • effect of temperature. Lactate dehydrogenase isoenzymes in developing tissues. Genetic variants of lactate dehydrogenase isoenzymes. Diagnostic applications of lactate dehydrogenase isoenzymes:myocardial infarction
  • liver diseases
  • malignant diseases
  • diseases of muscle
  • diseases of joints: anaemia
  • pregnancy
  • renal diseases
  • non-electrophoretic diagnostic techniques:serum 2-hydroxybutyrate dehydrogenase in diagnosis
  • relative heat-stability test
  • solvent-precipitation techniques
  • selective absorption techniques. Summary.- 7 Multiple Molecular Forms of Other Oxidoreductases.- Malate dehydrogenase: mitochondrial and supernatant malate dehydrogenase isoenzymes
  • biological significance of malate dehydrogenase isoenzymes
  • malate dehydrogenase isoenzymes in mammalian tissues
  • malate dehydrogenase isoenzymes in insect development
  • malate dehydrogenase isoenzymes of the chicken embryo. Isocitrate dehydrogenase: isocitrate dehydrogenase isoenzymes in heart and liver diseases. Glutamate dehydrogenase. Alcohol dehydrogenase: alcohol dehydrogenases of insects
  • avian alcohol dehydrogenases
  • alcohol dehydrogenases in mammalian liver
  • alcohol dehydrogenase polymorphism in plants. Xanthine dehydrogenase. Miscellaneous dehydrogenases.- 8 Aminotransferase (Transaminase) Isoenzymes.- Separation of aspartate aminotransferase isoenzymes. Properties of aspartate aminotransferase isoenzymes. Clinical applications of aspartate aminotransferase isoenzymes. Aspartate aminotransferase isoenzymes in developing tissues. Alanine aminotransferase.- 9 Phosphatase Isoenzymes.- Alkaline phosphatase: distribution, paper electrophoresis
  • starch-block electrophoresis
  • agar-gel electrophoresis
  • starchgel electrophoresis
  • acrylamide-gel electrophoresis
  • electrophoresis on Sephadex G-200
  • cellulose acetate electrophoresis
  • ion-exchange chromatography
  • properties of alkaline phosphatases
  • substrate affinities
  • effects of inhibitors
  • heat inactivation
  • effect of neuraminidase
  • summary of catalytic properties of tissue alkaline phosphatases
  • immunochemical reactions
  • genetic studies
  • alkaline phosphatase isoenzymes in bacteria. Acid phosphatase
  • electrophoretic separation
  • chromatographic investigations
  • genetic variants of human acid phosphatases.- 10 Multiple Forms of Esterases.- Aliesterases: genetic variations of non-specific esterases
  • ontogenetic observations. Cholinesterases: plasma cholinesterases
  • genetic polymorphism of serum cholinesterases
  • Cholinesterase isoenzymes in other species. Arylesterases:serum arylesterases
  • tissue esterases. Esterases and isoenzymes.- 11 Miscellaneous Enzymes.- Arylamidase: arylamidase isoenzymes in man
  • arylamidases in other species. Alanine aminopeptidase. Creatine kinase: creatine kinase isoenzymes. Arginine kinase. Caeruloplasmin (copper oxidase). Catalase. Carbonic anhydrase. Amylase: serum and tissue amylases
  • urinary amylase
  • macroamylasaemia. Other enzymes occurring in multiple forms: glycogen Phosphorylase
  • adenylate kinase
  • adenosine deaminase
  • tyrosinase
  • ribonuclease
  • deoxyribonucleic acid (DNA) polymerase
  • peroxidase
  • hyaluronate lyase (hyaluronidase)
  • ?-glycosidases.- 12 The Biological Significance of Isoenzymes.- Author Index.

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Details

  • NCID
    BA24462310
  • ISBN
    • 0412212706
  • Country Code
    uk
  • Title Language Code
    eng
  • Text Language Code
    eng
  • Place of Publication
    London
  • Pages/Volumes
    xii, 369 p
  • Size
    22 cm
  • Classification
  • Subject Headings
  • Parent Bibliography ID
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