Chattopadhyay T, Chatterjee B
Department of Biological Chemistry, Indian Association for the Cultivation of Science, Jadavpur, Calcutta, India.
Biochem Mol Biol Int. 1997 Jun;42(1):183-91. doi: 10.1080/15216549700202571.
The amino acid and carbohydrate analysis of scyllin, a low molecular weight lectin purified from Scylla serrata (edible crab) haemolymph reveal that scyllin is rich in acidic and neutral amino acids and contains high amount of mannose. UV absorption of scyllin is perturbed by DMSO at 272 nm showing the presence of tryptophan molecule in scyllin exposed and accessible to the solvent. The oxidation of tryptophan molecule by N-bromosuccinimide results in loss of haemagglutinating activity of lectin. The study of thermodynamic parameters of scyllin-glycoproteins interaction suggests that ceruloplasmin is the most potent inhibitors of scyllin of all the glycoproteins studied.
从锯缘青蟹（食用蟹）血淋巴中纯化得到的一种低分子量凝集素——锯缘青蟹凝集素（scyllin）的氨基酸和碳水化合物分析表明，锯缘青蟹凝集素富含酸性和中性氨基酸，且含有大量甘露糖。在272 nm处，二甲基亚砜（DMSO）会干扰锯缘青蟹凝集素的紫外吸收，这表明在锯缘青蟹凝集素中存在暴露于溶剂且可接触到的色氨酸分子。N-溴代琥珀酰亚胺对色氨酸分子的氧化导致凝集素的血凝活性丧失。对锯缘青蟹凝集素与糖蛋白相互作用的热力学参数研究表明，在所有研究的糖蛋白中，铜蓝蛋白是锯缘青蟹凝集素最有效的抑制剂。
