Raibekas A A
Institute of Biophysics, USSR Academy of Sciences, Krasnoyarsk.
J Biolumin Chemilumin. 1991 Jul-Sep;6(3):169-76. doi: 10.1002/bio.1170060306.
A green flavoprotein (GFP) was isolated and purified to homogeneity from Photobacterium leiognathi, strain 208. GFP is a homodimer of molecular weight 54,000 and contains two molecules of an unusual flavin per molecule of protein. Various biochemical characteristics including isoelectric point, trypsin and chymotrypsin degradation, SDS and temperature influence on subunit dissociation and the dissociation of the flavin chromophore, were investigated. The sequence of 23 N-terminal amino acids was determined and found to be concurrent with the N-terminal amino acid sequence encoded by the lux G(N) gene of P. leiognathi. This fact suggests that GFP is a structural component of the Photobacterium luminescence system.
从鱼发光杆菌208菌株中分离并纯化出一种绿色黄素蛋白（GFP），使其达到同质状态。GFP是一种分子量为54,000的同型二聚体，每个蛋白质分子含有两个不寻常的黄素分子。研究了各种生化特性，包括等电点、胰蛋白酶和胰凝乳蛋白酶降解、SDS和温度对亚基解离以及黄素发色团解离的影响。测定了23个N端氨基酸的序列，发现其与鱼发光杆菌lux G(N)基因编码的N端氨基酸序列一致。这一事实表明，GFP是鱼发光杆菌发光系统的一种结构成分。
