Sidler W, Gysi J, Isker E, Zuber H
Hoppe Seylers Z Physiol Chem. 1981 Jun;362(6):611-28. doi: 10.1515/bchm2.1981.362.1.611.
The amino acid sequences of the alpha- and beta-subunit of allophycocyanin, a water-soluble light-harvesting protein-pigment complex from the thermophilic cyanobacterium Mastigocladus laminosus have been determined. The alpha-chain consists of 160 amino acid residues and the beta-chain of 161 amino acid residues. The homology of the alpha- and beta-chains is 37%. A comparison with C-phycocyanin reveals that the second chromophore of the C-phycocyanin beta-subunit is attached to an inserted peptide of 10 amino acid residues at position 151-160.
已确定来自嗜热蓝细菌层理鞭枝藻的水溶性捕光蛋白色素复合物别藻蓝蛋白的α和β亚基的氨基酸序列。α链由160个氨基酸残基组成,β链由161个氨基酸残基组成。α链和β链的同源性为37%。与C-藻蓝蛋白的比较表明,C-藻蓝蛋白β亚基的第二个发色团连接到151-160位的10个氨基酸残基的插入肽上。