A new mannose/glucose-specific lectin, named DigL, was purified from seeds of Dialium guineense by a single step using a Sepharose 4b-Mannose affinity chromatography column. DigL strongly agglutinated rabbit erythrocytes and was inhibited by d-mannose, d-glucose, and derived sugars, especially α-methyl-d-mannopyranoside and N-acetyl-d-glucosamine. DigL has been shown to be a stable protein, maintaining its hemagglutinating activity after incubation at a wide range of temperature and pH values and after incubation with EDTA. DigL is a glycoprotein composite by approximately 2.9% of carbohydrates by weight. By sodium dodecyl sulfate polyacrylamide gel electrophoresis analysis, the purified DigL exhibited an electrophoretic profile consisting of a broad band of 28-30 kDa. Analysis using electrospray ionization mass spectrometry indicated that purified DigL possesses a molecular average mass of 28 452 ± 2 Da and shows the presence of possible glycoforms. In addition, DigL exhibited an intermediary toxic effect on Artemia sp. nauplii, and this effect was both dependent on native structure and mediated by a carbohydrate-binding site.

译文

:使用Sepharose 4b-甘露糖亲和色谱柱,只需一步即可从Dialial guineense种子中纯化出一种名为DigL的新型甘露糖/葡萄糖特异性凝集素。 DigL强烈凝集兔红细胞,并被d-甘露糖,d-葡萄糖和衍生糖,尤其是α-甲基-d-甘露吡喃糖苷和N-乙酰基-d-葡萄糖胺抑制。已经证明DigL是一种稳定的蛋白质,可以在很宽的温度和pH值范围内以及与EDTA一起孵育后保持其血凝活性。 DigL是糖蛋白复合物,约占碳水化合物重量的2.9%。通过十二烷基硫酸钠聚丙烯酰胺凝胶电泳分析,纯化的DigL显示出由28-30 kDa的宽带组成的电泳图谱。使用电喷雾电离质谱的分析表明,纯化的DigL的分子平均质量为28×452×±2×Da,并显示可能存在的糖型。另外,DigL对Artemia sp。表现出中间毒性作用。无节幼体,这种作用既取决于天然结构,又由碳水化合物结合位点介导。

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