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Luciferase ofLuciola mingrelica fireflies. Kinetics and regulation mechanism

โœ Scribed by Ugarova, N. N.

Publisher
John Wiley and Sons
Year
1989
Weight
932 KB
Volume
4
Category
Article
ISSN
0884-3996

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โœฆ Synopsis

Biochemical properties, spectral parameters of bioluminescence and reaction kinetics for Luciola mingrelica firefly luciferase are described and analysed. The kinetic scheme of the enzymatic process is proposed and discussed. Allosteric regulation of luciferase activity by ATP and its analogues is considered and binding Mg2+ t o luciferase shown t o increase its activity. Regulation mechanism of luciferase activity by phospholipids is analysed and choline-containing phospholipids shown t o be specific luciferase activators. Some properties of firefly luciferase and the luciferase synthesized during firefly mRNA translation in frog oocytes are compared.

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Crude and purified firefly luciferase have been used to assay ATP from 0.2 pmol to 2 pmol. Over this range of ATP concentrations, there is a large change in the kinetics of light emission. At the lowest concentrations of ATP, light emission rises to a maximum and remains constant for a minute or lon