Sidler W, Kumpf B, Suter F, Morisset W, Wehrmeyer W, Zuber H
Biol Chem Hoppe Seyler. 1985 Mar;366(3):233-44. doi: 10.1515/bchm3.1985.366.1.233.
The N-terminal amino-acid sequences of two green alpha-subunit fractions from Chroomonas phycocyanin-645 and from two violet alpha-subunit fractions from Cryptomonas phycoerythrin-545 reveal that these cryptomonad biliproteins each contain two different alpha-subunits. The chromophore binding sites at the cysteine residues in positions 18 or 19 are homologous to the chromophore binding site at cysteine position 84 in cyanobacterial biliproteins. The sequence homologies of the beta-subunits to cyanobacterial biliproteins are higher than those of the alpha-subunits. Cryptomonas phycoerythrin-545 alpha-subunits contain a gamma-hydroxylysine residue at the fourth position of the polypeptide chains. 50%-75% of the total sequence of the alpha-subunits was determined by N-terminal amino-acid sequence analysis. The alpha-subunits of the Cryptomonad biliproteins are smaller than the alpha-subunits of the cyanobacterial biliproteins. Comparing sequence homologies we found 60 amino-acid residues less at the N-terminus of Cryptomonad biliproteins than in cyanobacterial biliproteins.
来自蓝隐藻藻蓝蛋白-645的两种绿色α亚基组分以及来自隐甲藻藻红蛋白-545的两种紫色α亚基组分的N端氨基酸序列表明，这些隐甲藻双蛋白各自包含两种不同的α亚基。第18或19位半胱氨酸残基处的发色团结合位点与蓝细菌双蛋白中第84位半胱氨酸处的发色团结合位点同源。β亚基与蓝细菌双蛋白的序列同源性高于α亚基。隐甲藻藻红蛋白-545的α亚基在多肽链的第四个位置含有一个γ-羟基赖氨酸残基。通过N端氨基酸序列分析确定了α亚基总序列的50%-75%。隐甲藻双蛋白的α亚基比蓝细菌双蛋白的α亚基小。比较序列同源性时，我们发现隐甲藻双蛋白N端的氨基酸残基比蓝细菌双蛋白少60个。
