A novel lectin from the sponge Haliclona cratera:: isolation, characterization and biological activity
A novel lectin from the sponge Haliclona cratera:: isolation, characterization and biological activity
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DOI：
10.1016/s1532-0456(02)00068-6
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发表时间：
2002-06-01
影响因子：
3.9
通讯作者：
Gasic, MJ
中科院分区：
文献类型：
--
作者：
Pajic, I;Kljajic, Z;Gasic, MJ
用离子交换和凝胶层析法从亚得海海绵Haliclona cratera中分离纯化出一种凝集素，其分子质量约为29 kDa。纯化的凝集素富含疏水性氨基酸和碱性氨基酸，等电点为pH 8.6。克伦特拉凝集素具有较高的热稳定性和pH稳定性。它能凝集天然和胰酶、木瓜蛋白酶和神经氨酸酶处理的人的A、B、O、AB和绵羊红细胞，其血凝活性不受钙、锰和镁离子的影响，D-半乳糖和N-乙酰-D-氨基半乳糖是该活性的中度抑制剂。克氏梭菌凝集素对HeLa和FemX细胞有细胞毒作用，对植物血凝素(PHA)处理的人T淋巴细胞有微弱的促有丝分裂作用。(C)2002 Elsevier Science Inc.保留所有权利。
A lectin from the Adriatic sponge Haliclona cratera was purified by ion-exchange and gel chromatography The molecular mass of the lectin is approximately 29 kDa. Purified lectin is rich in hydrophobic and basic amino acids and has an isoelectric point at pH 8.6. H. cratera lectin is relatively heat- and pH-stable. It agglutinates native and trypsinized, papainized and neuraminidase-treated human A, B, O, AB and sheep erythrocytes, and the hemagglutinating activity is independent of Ca2+, Mn2+ and Mg2+ ions; D-galactose and N-acetyl-D-galactosamine are found to be moderate inhibitors of the activity. H. cratera lectin displays cytotoxic effect on HeLa and FemX cells and weak mitogenic effect on human T-lymphocytes pretreated with phytohemagglutinin (PHA). (C) 2002 Elsevier Science Inc. All rights reserved.