Sampaio A H, Rogers D J, Barwell C J
Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Brasil.
Phytochemistry. 1998 Jul;48(5):765-9. doi: 10.1016/s0031-9422(97)00966-7.
A lectin from the red marine alga Ptilota filicina (PFL) was isolated by affinity chromatography on cross-linked guar gum. PFL agglutinated native and papain-treated human erythrocytes with preference for type O erythrocytes. The lectin was inhibited by galactose and its derivatives. The most potent inhibitors were p-Nitrophenyl-N-acetyl-alpha- and beta-D-galactosaminide. Porcine stomach mucin, bovine submaxillary gland mucin and asialo bovine mucin were also inhibitory. The M(r) of PFL, determined by gel filtration, was 56,900. SDS-PAGE gave one band with a subunit M(r) of 19,320, indicating the native protein to be a trimer of apparently identical subunits. PFL was shown to be rich in acidic and hydroxyl amino acids but low in basic amino acids. The ten N-terminal amino acids were Asx-Thr-Lys-Thr-Leu-Leu-Ala-.
通过在交联瓜尔胶上进行亲和层析,从红色海藻丝状羽藻(Ptilota filicina,PFL)中分离出一种凝集素。PFL能凝集天然的和经木瓜蛋白酶处理的人红细胞,对O型红细胞有偏好。该凝集素受到半乳糖及其衍生物的抑制。最有效的抑制剂是对硝基苯基 - N - 乙酰 - α - 和β - D - 半乳糖胺。猪胃粘蛋白、牛颌下腺粘蛋白和去唾液酸牛粘蛋白也具有抑制作用。通过凝胶过滤测定,PFL的分子量为56,900。SDS - PAGE显示有一条带,亚基分子量为19,320,表明天然蛋白是由明显相同的亚基组成的三聚体。结果表明PFL富含酸性和羟基氨基酸,但碱性氨基酸含量较低。其N端的十个氨基酸为Asx - Thr - Lys - Thr - Leu - Leu - Ala - 。