UID:
almafu_9960141376302883
Umfang:
1 online resource (710 p.)
Ausgabe:
Reprint 2021
ISBN:
9783112575024
Anmerkung:
Frontmatter --
,
WELCOME ADDRESS --
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CONTENTS --
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I. ENZYMATIC HYDROLYSIS OF INORGANIC PHOSPHATES --
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Hydrolysis of the substrates by inorganic pyrophosphatase from yeast --
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On the origin of inorganic pyrophosphatase obtained from bakers' yeast --
,
Dissociation and association behavior of inorganic pyrophosphatase from bakers' yeast --
,
On the state of aromatic amino acids in inorganic pyrophosphatase from bakers' yeast --
,
Phosphotransferase reactions in the inorganic polyphosphate metabolism --
,
The study of polyphosphate depolymerase of Neurospora crassa --
,
Some properties of a polyphosphatase from Endomyces magnusii --
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Some properties of polyphosphatase from Neurospora crassa --
,
Localization of polyphosphates and polyphosphatases in Neurospora crassa --
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On a possibility of non-enzymatic transphosphorylation by highpolymeric polyphosphate --
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On the regulation of some enzymes of phosphorous metabolism in E. coli --
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Significance of repressible polyphosphate phosphohydrolases in yeast and higher plants --
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2. ADENOSINTRIPHOSPHATASE --
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Some properties of the soluble mitochondrial ATPase --
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The identification of ionic form of phosphate accompanying active Ca2+uptake in rat liver mitochondria --
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Mechanism of activation of myosin adenosinetriphosphatase by actin --
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Transfer ATPase of muscle membranes --
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018-exchange reaction as a test in the studing of the phosphoryl groups transport from ATP to myosin --
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Phosphorylated derivates of histidine containing dipeptides, their synthesis and physiological role --
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Na-K activated ATPase and active cation transport --
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Anion effects on Mg-activated ATPase of Lizard gastric mucosa --
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Inorganic pyrophosphatase in developing teeth: effects of Magnesium and diphosphonates --
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Does Na+ + K+ - dependent ATPase consist of more than one enzyme entity? --
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Binding of ATP to (Na+ + K+ ) activated ATPase. Number of binding sites and enzyme-ATP dissociation constant --
,
Some properties of ATPase from plant tissues --
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The interaction of monosaccharides with intestinal (Na+ - K+) - ATPase --
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Monosaccharide dependent Na+ -fluxes across intestinal epithelium and their possible relations to (Na+ - K+) -ATPase --
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3. MECHANISM OF ACTION AND CONTROL PROPERTIES OF SELECTED ENZYME SYSTEMS IN MAIN ROUTES OF METABOLISM --
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General Problems --
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Regulation of enzymes by phosphorylation and adenylylation --
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Allosteric effects by products and substrates involving specifically regulatory sites --
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Regulation of enzymic activity by intra - and inter-subunit interactions --
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Selected Enzymes --
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The function of pyridoxal-5' -phosphate in glycogen Phosphorylase --
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Conformational changes upon binding of PLP, PLP-analogues and 5' -AMP to the apoenzyme of rabbit skeletal muscle Phosphorylase b --
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About allosteric interactions on Phosphorylase b from muscle --
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Allosterische Eigenschaften der Glykogenphosphorylase b aus Herzund Skelettmuskel des Schweins - eines gemischten V, K-Enzymsystems --
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Isoenzyme der Phosphorylase b im Herzmuskel des Schweines: einige Aspekte zur Regulation der Glykogenolyse --
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Structure and catalytic mechanisms of some hexokinases --
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Lokalisierung und Eigenschaften der Hexokinase pflanzlicher Gewebe --
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Unsolved problems of phosphofructokinase --
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Relations between structure and catalytic activity of rabbit muscle phosphofructokinase --
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Interconversion of two forms of yeast phosphofructokinase --
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Influence of effectors on the molecular properties and enzymic activity of yeast phosphofructokinase --
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Isolation and characterization of fructose diphosphate aldolase from beef muscle --
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Studies on subunit structure of erythrocyte phosphofructokinase --
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Significance of the PFK-reaction for the regulation of glycolysis --
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Regulation of fructose-1, 6-diphosphatase in yeasts, inactivation by glucose --
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Mechanisms of enzymatic aldol cleavage of fructose-6-phosphate --
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Interaction and dissimilarity of subunits of glyceraldehyde-3-phosphate dehydrogenase --
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Kinetic properties of glyceraldehyde-phosphate dehydrogenase from erythrocytes --
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Structure and function of pyruvate kinase --
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PH-function and allosteric control of yeast pyruvate kinase --
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The alterations of isoenzymogram of lactatdehydrogenase in rabbits by synthetic estrogen --
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4. ENZYMATIC SYNTHESIS AND SPLITTING OF RIBONUCLEIC ACID --
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Positive Control of RNA synthesis --
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Structure, function and modification of the DNA-dependent RNA-polymerase from E. coli --
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DNA-dependent RNA polymerase: properties of the ribonucleoside triphosphates binding sites as revealed by inhibition studies with substrate analogues --
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DNA-dependent RNA polymerase inhibition by L-ATP --
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The study of substrate specificity of polynucleotide phosphorylase (Streptomyces aureofaciens) --
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5. SPECIAL TOPICS --
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The use of modified nucleotide derivates for the study of some nucleolytic enzymes --
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Catalytic principles used in the reaction of RNase A, T1 and T2 with substrates --
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The specific ribonuclease from Streptomyces aureofaciens --
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Some properties of extracellular RNases of fungi --
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Thermodynamics of the adenylylation of glutamine synthetase --
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Temperature dependence of creatine kinase activity --
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The behavior of transferases in heterogenic lipid-water systems --
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A general computer strategy for the analysis of kinetic and binding curves --
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Kinetic investigations of enzymes with substrates forming metal complexes --
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Interaction of imidazole with multivalent anions a s model for binding of phosphocompounds to proteins --
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Enhanced reactivity of the SH-group of thiol-subtilisin --
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Ursprung und Eigenschaften von Isozymen der Phosphomonoesterasen --
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Ligandinduzierte Änderungen von CD-Spektren und vom Assoziations- Dissoziations-Gleichgewicht des Neunaugen-Hämoglobins --
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Properties of a high molecular aryl-amidase-phosphatase-complex from rat kidney microsomes and attempts for the separation of both enzyme activities --
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ACTIVE MEMBERS OF THE SYMPOSIUM
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In English.
Weitere Ausg.:
ISBN 9783112575017
Sprache:
Englisch
DOI:
10.1515/9783112575024
URL:
https://doi.org/10.1515/9783112575024
URL:
https://www.degruyter.com/isbn/9783112575024
URL:
https://doi.org/10.1515/9783112575024
URL:
https://www.degruyter.com/isbn/9783112575024