萤火虫（Luciola cruciata和Luciola lateralis）荧光素酶的纯化与特性分析
Purification and characterization of luciferases from fireflies, Luciola cruciata and Luciola lateralis.
作者信息
Kajiyama N, Masuda T, Tatsumi H, Nakano E
机构信息
Research and Development Division, Kikkoman Corporation, Chiba, Japan.
出版信息
Biochim Biophys Acta. 1992 Apr 8;1120(2):228-32. doi: 10.1016/0167-4838(92)90275-i.
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. LlL was superior to LcL and PpL in thermal and pH stability, and the reaction catalyzed by LlL emits green light with a peak intensity at 552 nm, which is 10 nm shorter in wavelength than those of PpL and LcL.
通过硫酸铵沉淀、凝胶过滤柱色谱法和羟基磷灰石高效液相色谱法，将黑翅萤（Luciola cruciata）和黄缘萤（Luciola lateralis）的荧光素酶LcL和LlL纯化至同质。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳（SDS-PAGE）测定的这两种酶的分子量均为62 kDa，与萤火虫（Photinus pyralis，PpL）的分子量几乎相同。发现LcL在热稳定性、pH稳定性和最大光强度波长方面与PpL相似。LlL在热稳定性和pH稳定性方面优于LcL和PpL，并且由LlL催化的反应发出绿光，峰值强度在552 nm，其波长比PpL和LcL的波长短10 nm。
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