Methods in Enzymology Vol.133 Bioluminescence and Chemiluminescence, Part B

This chapter discusses determination of cloning firefly luciferase. Firefly luciferase catalyzes the ATP-dependent oxidative decarboxylation of luciferin (LH2) resulting in the production of light. The most well characterized firefly luciferase is isolated from the common North American firefly Photinus pyralis. Isolating luciferase cDNA clones will allow the determination of the nucleotide sequence of this gene from which the amino acid sequence of the enzyme can be deduced. When the luciferase genes of other species of fireflies are cloned, comparison of their sequences can help pinpoint regions of the enzyme that are essential to its function and increase our understanding of bioluminescent reactions. The cloning of luciferase cDNA and the expression of the enzyme in an active form in Escherichia coli, and would provide an unlimited source of this enzyme. Cloned luciferase cDNA could be very useful for the monitoring of gene expression. The simple and sensitive assay for luciferase may allow the in vivo detection of this enzyme obviating the need to destroy the cells being monitored. As this is a single gene system, it is likely to be particularly useful in eukaryotic systems as an indicator of promoter activity in plant, animal, and lower eukaryote cells using both in vitro and in vivo tests.

• Series: Bioluminescence & Chemiluminescence
• Hardcover: 649 pages
• Publisher: Academic Press (January 11, 1987)
• Language: English
• ISBN-10: 0121820335
• ISBN-13: 978-0121820336
• Product Dimensions: 9.1 x 6.4 x 1.3 inches

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