Jirgensons B
Biochim Biophys Acta. 1978 Sep 26;536(1):205-11. doi: 10.1016/0005-2795(78)90066-1.
Conformation and conformational transitions of phytohemagglutinins (lectins) from Arachis hypogaea (peanut), Lens culinaris (lentil), Glycine max (soybean), and Ricinus communis (castor bean) were studied by the circular dichroism probe. The lectins were found to possess a high amount of the pleated sheet (beta) conformation. The tertiary structure and main chain conformation of the lectins were disorganized by sodium dodecyl sulfate (SDS) and the main chain was reconstructed by relatively high concentrations of SDS (weight ratio of SDS to protein about 5-8 to 1) into new orders of higher helix content than in the native protein. More helix was formed in acid solutions than in nearly neutral solutions. The disorganization of the native tertiary structure by SDS was expressed in a decrease of the circular dichroism bands related to the tyrosine and tryptophan chromophores and in appearance of the vibronic fine structure in the phenylalanine band zone. The tertiary structure of the L. culinaris and R. communis lectins was more sensitive to SDS than the tertiary structure of the two other lectins.
利用圆二色性探针研究了来自花生、小扁豆、大豆和蓖麻的植物血凝素（凝集素）的构象及构象转变。发现这些凝集素具有大量的β折叠构象。十二烷基硫酸钠（SDS）会破坏凝集素的三级结构和主链构象，而相对高浓度的SDS（SDS与蛋白质的重量比约为5 - 8比1）会将主链重构成比天然蛋白质具有更高螺旋含量的新结构。在酸性溶液中比在近中性溶液中形成更多的螺旋。SDS对天然三级结构的破坏表现为与酪氨酸和色氨酸发色团相关的圆二色性谱带的降低以及苯丙氨酸谱带区域中振动精细结构的出现。小扁豆和蓖麻凝集素的三级结构比其他两种凝集素的三级结构对SDS更敏感。
