Comparison of properties of commercially available crystalline native and recombinant firefly luciferases.
Commercially available crystalline native and recombinant firefly luciferases were compared. The two types of luciferase had indistinguishable responses to variation in ATP and luciferin concentrations and to omission of reaction components. The time courses of light production, the responses to nucleotide analogues, and the stability of the enzymes under several storage conditions were identical. The native enzyme had a slightly greater specific activity and was more sensitive to trypsin degradation. These differences are probably attributable to differences in conformation.
Ford
S R
SR
Department of Biochemistry, Oklahoma State University, Stillwater 74078-0454.
Hall
M S
MS
Leach
F R
FR
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001517:Coleoptera; D007700:Kinetics; D008027:Light; D008156:Luciferases / Q000378:metabolism*; D009711:Nucleotides / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D009711:Nucleotides; D011994:Recombinant Proteins; D000255:Adenosine Triphosphate; D008156:Luciferases