Dam T K, Bandyopadhyay P, Sarkar M, Ghosal J, Bhattacharya A, Choudhury A
Department of Marine Science, University of Calcutta, India.
Biochem Biophys Res Commun. 1994 Aug 30;203(1):36-45. doi: 10.1006/bbrc.1994.2145.
The heparin-binding lectin, Anadarin MS, from the plasma of the marine clam Anadara granosa is purified through affinity chromatography on heparin-Sepharose 4B followed by gel filtration on a Sepharose 6B column. The purified lectin is a pentameric protein of native M(r) 300 kDa and is composed of identical subunits of 60 kDa. The pI value of this Ca(2+)-dependent lectin is 6.2. Anadarin MS agglutinates normal rabbit erythrocytes but not that of human. Aspartic acid, glutamic acid, histidine and glycine are the predominant amino acids. Unlike other reported heparin-binding lectins, Anadarin MS exhibits a unique and strict specificity for iduronic acid containing glycosaminoglycans. This lectin agglutinates infective promastigotes of Leishmania donovani exclusively and can therefore be used as a novel biochemical surface marker for this parasite.
从海生蚶类泥蚶血浆中提取的肝素结合凝集素Anadarin MS，先通过肝素-琼脂糖4B亲和层析进行纯化，然后在琼脂糖6B柱上进行凝胶过滤。纯化后的凝集素是一种天然相对分子质量为300 kDa的五聚体蛋白，由相同的60 kDa亚基组成。这种钙依赖性凝集素的等电点值为6.2。Anadarin MS能凝集正常兔红细胞，但不能凝集人红细胞。天冬氨酸、谷氨酸、组氨酸和甘氨酸是主要氨基酸。与其他已报道的肝素结合凝集素不同，Anadarin MS对含艾杜糖醛酸的糖胺聚糖表现出独特而严格的特异性。这种凝集素仅能凝集杜氏利什曼原虫的感染性前鞭毛体，因此可作为该寄生虫的一种新型生化表面标志物。
