Lundell D J, Yamanaka G, Glazer A N
J Cell Biol. 1981 Oct;91(1):315-9. doi: 10.1083/jcb.91.1.315.
A rapid procedure is described for the isolation of "linker" polypeptides (Lundell, D. J., R. C. Williams, and A. N. Glazer. 1981. J. Biol. Chem. 256:3580-3592) of cyanobacterial phycobilisomes. The 75,000-dalton component of the core of Synechococcus 6301 phycobilisomes isolated by this procedure has been shown to carry a bilin similar in spectroscopic properties to phycocyanobilin. "Renatured" 75,000-dalton polypeptide has absorption maxima at 610 and 665 nm and a fluorescence emission maximum at 676 nm, similar to that of intact phycobilisomes. A complex of allophycocyanin and a 40,000-dalton bilin-carrying fragment of the 75,000-dalton polypeptide, obtained by limited tryptic digestion, is described. This complex, which lacks allophycocyanin B, shows a fluorescence emission maximum at 676 nm. The above data indicate that the 75,000-dalton polypeptide functions as a terminal energy acceptor in the phycobilisome.
本文描述了一种快速分离蓝藻藻胆体“连接”多肽的方法（伦德尔，D. J.，R. C. 威廉姆斯，和 A. N. 格雷泽。1981年。《生物化学杂志》256:3580 - 3592）。通过该方法分离出的聚球藻6301藻胆体核心的75,000道尔顿组分已被证明携带一种与藻蓝胆素光谱性质相似的胆素。“复性”的75,000道尔顿多肽在610和665纳米处有吸收最大值，在676纳米处有荧光发射最大值，类似于完整藻胆体。本文还描述了通过有限胰蛋白酶消化获得的别藻蓝蛋白与75,000道尔顿多肽的40,000道尔顿携带胆素片段的复合物。该复合物缺乏别藻蓝蛋白B，在676纳米处有荧光发射最大值。上述数据表明75,000道尔顿多肽在藻胆体中作为末端能量受体发挥作用。
