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Purification and properties of Renilla reniformis luciferase

Matthews, John C ; Hori, Kazuo ; Cormier, Milton J

Biochemistry (Easton), 1977-01, Vol.16 (1), p.85-91 [Peer Reviewed Journal]

United States: American Chemical Society

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Title:
Purification and properties of Renilla reniformis luciferase
Author: Matthews, John C ; Hori, Kazuo ; Cormier, Milton J
Subjects: 550200 - Biochemistry ; Amino Acids - analysis ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; CENTRIFUGATION ; CHEMICAL PROPERTIES ; CHROMATOGRAPHY ; CNIDARIA ; Cnidaria - enzymology ; ELECTROPHORESIS ; ENZYMES ; INVERTEBRATES ; Kinetics ; LUCIFERASE ; Luciferases - isolation & purification ; Luciferases - metabolism ; LUMINESCENCE ; Luminescent Measurements ; MOLECULAR STRUCTURE ; Molecular Weight ; ORGANIC COMPOUNDS ; OXIDASES ; OXIDOREDUCTASES ; PROTEINS ; PURIFICATION ; SEPARATION PROCESSES ; Spectrophotometry, Ultraviolet ; ULTRACENTRIFUGATION
Is Part Of: Biochemistry (Easton), 1977-01, Vol.16 (1), p.85-91
Notes: istex:619F446C4E8D3CAA250C56090319F4CA039C9EC9
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ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
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Description: Luciferase from the anthozoan coelenterate Renilla reniformis (Renilla luciferin:oxygen 2-oxidoreductase (decarboxylating), EC 1.13.12.5.) catalyzes the bioluminescent oxidation of Renilla luciferin producing light (lambdaB 480 nm, QB 5.5%), oxyluciferin, and CO2 (Hori, K., Wampler, J.E., Matthews, J.C., and Cormier, M.J. (1973), Biochemistry 12, 4463). Using a combination of ion-exchange, molecular-sieve, sulfhydryl-exchange, and affinity chromatography, luciferase has been purified, approximately 12 000-fold with 24% recovery, to homogeneity as judged by analysis with disc and sodium dodecyl sulfate-polyacrylamide gel electrophoresis, gel filtration, and ultracentrifugation. Renilla luciferase is active as a nearly spherical single polypeptide chain monomer of 3.5 X 10(4) daltons having a specific activity of 1.8 X 10(15) hp s-1 mg-1 and a turnover number of 111 mumol min-1 mumol-1 of enzyme. This enzyme has a high content of aromatic and hydrophobic amino acids such that it has an epsilon280nm 0.1% of 2.1 and an average hydrophobicity of 1200 cal residue-1. The high average hydrophobicity of luciferase, which places it among the more hydrophobic proteins reported, is believed to account, at least in part, for its tendency to self-associate forming inactive dimers and higher molecular weight species.
Publisher: United States: American Chemical Society
Language: English

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Purification and properties of Renilla reniformis luciferase

Matthews, John C ; Hori, Kazuo ; Cormier, Milton J

United States: American Chemical Society

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