Shimomura O, Flood P R
Biol Bull. 1998 Jun;194(3):244-252. doi: 10.2307/1543094.
Two types of luciferase that catalyze the luminescent oxidation of coelenterazine were isolated from the marginal exumbrella epithelium (lappet) and the ovary of Periphylla periphylla; they were designated luciferase-L and luciferase-O, respectively. Luciferase-L (Mr 32,000), probably derived from highly specialized photocytes, was very resistant to heat, and its activity was little affected by boiling; but it was unstable in solutions of low ionic strength if bovine serum albumin was not included in the solvent. Luciferase-O (Mr 75,000) occurred in the eggs in association with particulate matter, and was solubilized and extracted with a buffer containing 2 M guanidine hydrochloride; the enzyme was highly stable in this strongly denaturing solvent. The intensities of the coelenterazine luminescence catalyzed by both luciferases were maximal at pH 7.8 and in the presence of about 1 M NaCl. The quantum yield of coelenterazine was estimated to be 0.14 with luciferase-L (emission max. at 465 nm) and 0.12 with luciferase-O (emission max. at 470 nm). The luminescence caused by both luciferases was strongly inhibited by Cu2+ and thiol compounds.
从缘膜外伞上皮（叶状体）和仙女杯的卵巢中分离出两种催化腔肠素发光氧化的荧光素酶；它们分别被命名为荧光素酶-L和荧光素酶-O。荧光素酶-L（分子量32,000）可能源自高度特化的发光细胞，对热非常耐受，煮沸对其活性影响很小；但如果溶剂中不包含牛血清白蛋白，它在低离子强度溶液中不稳定。荧光素酶-O（分子量75,000）存在于与颗粒物质相关的卵中，并用含有2 M盐酸胍的缓冲液溶解和提取；该酶在这种强变性溶剂中高度稳定。两种荧光素酶催化的腔肠素发光强度在pH 7.8和约1 M NaCl存在下最大。荧光素酶-L催化时腔肠素的量子产率估计为0.14（发射最大值在465 nm），荧光素酶-O催化时为0.12（发射最大值在470 nm）。两种荧光素酶引起的发光都受到Cu2+和硫醇化合物的强烈抑制。
