Gardner E E, Stevens S E, Fox J L
Biochim Biophys Acta. 1980 Jul 24;624(1):187-95. doi: 10.1016/0005-2795(80)90237-8.
The C-phycocyanin from the marine blue-green alga, Agmenellum quadruplicatum, has been isolated and purified to electrophoretic homogeneity. This is the first C-phycocyanin for which a low resolution three dimensional structure has been published (Hackert, M.L., Abad-Zapatero, C., Stevens, S.E. Jr. and Fox, J.L. (1977), J. Mol. Biol. 111, 365-369 and Abad-Zapatero, C., Fox, J.L. and Hackert, M.L. (1977) Biochem. Biophys. Res Commun. 78, 266-272). The native C-phycocyanin complex shows an absorption maximum at 622 nm and another peak at 355 nm. In urea solutions, the 622 nm maximum of whole C-phycocyanin is shifted to 662 nm. Am662 = 94400 was determined. The fluorescence emission maxima at 650 nm for haloprotein is shifted and largely quenched in acid urea. The monomeric protein consists of two polypeptide chains with molecular weights of 16,000 for the alpha chain and 18,500 for the beta chain. Spectra in 8 M urea indicate that the alpha chain possesses one and the beta chain two phycocyanobilin chromophores. The isolated chains show absorption maxima at 622 nm for the alpha chain and 608 nm for the beta chain. Amino acid compositions of the holoprotein and the separated chains are given and N-terminal amino acid sequences are presented.
已从海洋蓝绿藻四聚顶丝藻中分离并纯化出C-藻蓝蛋白，使其达到电泳纯。这是首个已发表低分辨率三维结构的C-藻蓝蛋白（哈克特，M.L.，阿瓦德-萨帕特罗，C.，小史蒂文斯，S.E.和福克斯，J.L.（1977年），《分子生物学杂志》111卷，365 - 369页；以及阿瓦德-萨帕特罗，C.，福克斯，J.L.和哈克特，M.L.（1977年），《生物化学与生物物理研究通讯》78卷，266 - 272页）。天然C-藻蓝蛋白复合物在622纳米处有最大吸收峰，在355纳米处有另一个峰。在尿素溶液中，完整C-藻蓝蛋白的622纳米最大吸收峰移至662纳米。测定得ΔA662 = 94400。卤蛋白在650纳米处的荧光发射最大值在酸性尿素中发生位移并大幅淬灭。单体蛋白由两条多肽链组成，α链分子量为16000，β链分子量为18500。8M尿素中的光谱表明，α链含有一个藻蓝胆素发色团，β链含有两个藻蓝胆素发色团。分离出的链在α链的622纳米和β链的608纳米处有最大吸收峰。给出了全蛋白和分离链的氨基酸组成，并列出了N端氨基酸序列。
