COMPARISON OF PROPERTIES OF COMMERCIALLY AVAILABLE CRYSTALLINE NATIVE AND RECOMBINANT FIREFLY LUCIFERASES

被引：4

作者：

FORD, SR ^{[1
]}

HALL, MS ^{[1
]}

LEACH, FR ^{[1
]}

机构：

[1] OKLAHOMA STATE UNIV,DEPT BIOCHEM,STILLWATER,OK 74078

来源：

JOURNAL OF BIOLUMINESCENCE AND CHEMILUMINESCENCE | 1992年 / 7卷 / 03期

关键词：

FIREFLY LUCIFERASE; TRYPSIN DEGRADATION; ATP; BIOLUMINESCENCE; RECOMBINANT FIREFLY LUCIFERASE;

D O I：

10.1002/bio.1170070305

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：185 / 193

页数：9

共 36 条

[1] REPORTER GENES - APPLICATION TO THE STUDY OF MAMMALIAN GENE-TRANSCRIPTION [J].