Cohen-Bazire G, Béguin S, Rimon S, Glazer A N, Brown D M
Arch Microbiol. 1977 Jan 11;111(3):225-38. doi: 10.1007/BF00549359.
Allophycocyanins were purified from diverse cyanobacteria and one rhodophytan alga (Cyanidium caldarium). The native proteins are trimeric molecules with the structure (alpha beta)3. Representative native allophycocyanins and their alpha and beta subunits were characterized with respect to molecular weight, amino acid composition, isoelectric point, absorption and fluorescence spectra and immunological properties. All of the allophycocyanins studied were strikingly similar with respect to each of these properties. Renatured alpha and beta subunits of allophycocyanin were distinct immunologically from each other, and both cross-reacted with the antiserum to the native protein. Trimeric allophycocyanin was readily reconstituted from the purified alpha and beta subunits. Formation of hybrid allophycocyanins was demonstrated by direct isolation and characterization of the hybrid proteins and by immunological techniques. The results support the view that allophycocyanins are a highly conserved group of proteins.
别藻蓝蛋白是从多种蓝细菌和一种红藻(嗜热蓝藻)中纯化得到的。天然蛋白质是具有(αβ)3结构的三聚体分子。对代表性的天然别藻蓝蛋白及其α和β亚基进行了分子量、氨基酸组成、等电点、吸收光谱和荧光光谱以及免疫学性质的表征。所研究的所有别藻蓝蛋白在这些性质的每一方面都极为相似。别藻蓝蛋白复性的α和β亚基在免疫学上彼此不同,但二者均与针对天然蛋白的抗血清发生交叉反应。三聚体别藻蓝蛋白很容易从纯化的α和β亚基重新组装而成。通过对杂交蛋白的直接分离和表征以及免疫学技术证明了杂交别藻蓝蛋白的形成。这些结果支持了别藻蓝蛋白是一组高度保守的蛋白质的观点。