Isolation and properties of prostaglandin H synthetase immobilized in insoluble polyelectrolyte complexes

Immobilization of prostaglandin-H-synthetase (EC 1.14.99.1) of the microsomal fraction of ram vesicular gland in the microparticles of insoluble polyelectrolyte complexes by non-covalent incorporation was studied. It was shown that immobilization occurs with a high efficiency and high activity yield...

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Bibliographic Details
Published inBiokhimiia (Moscow, Russia) Vol. 51; no. 8; p. 1268
Main Authors Kirpotin, D B, Motorin, Iu A, Mevkh, A T, Varfolomeev, S D, Orlovskiĭ, A F
Format Journal Article
LanguageRussian
Published Russia (Federation) 01.08.1986
Subjects
Animals
Arachidonic Acid
Arachidonic Acids - metabolism
Cattle
Enzymes, Immobilized
Hydrogen-Ion Concentration
Kinetics
Polyamines
Polymers
Prostaglandin-Endoperoxide Synthases - isolation & purification
Prostaglandin-Endoperoxide Synthases - metabolism
Sheep
Temperature
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Summary:Immobilization of prostaglandin-H-synthetase (EC 1.14.99.1) of the microsomal fraction of ram vesicular gland in the microparticles of insoluble polyelectrolyte complexes by non-covalent incorporation was studied. It was shown that immobilization occurs with a high efficiency and high activity yield (40-70%). Non-specific reversible inhibition of the enzyme by the polycationic component of the complex was demonstrated. The dependencies of activity of the native and immobilized enzymes on pH, temperature and substrate (adrenaline and arachidonic acid) were studied. The immobilized enzyme had an increased thermal stability as compared to the native one; the thermoinactivation rate constant was decreased 3-7 times. The biexponential type of the curve of the rependence of activity vs. time for the native enzyme and the transformation of the curve into a simple exponential form for the immobilized enzyme were observed.
ISSN:0320-9725