PURIFICATION AND CHARACTERIZATION OF LUCIFERASES FROM FIREFLIES, LUCIOLA-CRUCIATA AND LUCIOLA-LATERALIS

被引：31

作者：

KAJIYAMA, N

MASUDA, T

TATSUMI, H

NAKANO, E

机构：

[1] Research and Development Division, Kikkoman Corporation, Noda-city, Chiba

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1992年 / 1120卷 / 02期

关键词：

FIREFLY LUCIFERASE; THERMAL STABILITY; (L-CRUCIATA); (L-LATERALIS);

D O I：

10.1016/0167-4838(92)90275-I

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：

Luciferases of Luciola cruciata and Luciola lateralis, LcL and LlL, were purified to homogeneity by ammonium sulfate precipitation, gel-filtration column chromatography, and hydroxyapatite HPLC. The molecular masses of the enzymes determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) were both 62 kDa, almost identical to that of Photinus pyralis (PpL). LcL was found to be similar to PpL in thermal stability, pH stability, and the wavelength of maximum light intensity. LIL was superior to LcL and PpL in thermal and pH stability, and the reaction catalyzed by LIL emits green light with a peak intensity at 552 nm, which is 10 nm shorter in wavelength than those of PpL and LcL.

引用

页码：228 / 232

页数：5

共 22 条

[1] SEPARATION OF FIREFLY LUCIFERASE USING AN ANION-EXCHANGER [J].