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采用ELISA技术,建立人甘露聚糖结合凝集素(MBL)与MBL相关丝氨酸蛋白酶(MASP)结合的检测体系。设计合成一系列MBL胶原样区(CLR)的相应短肽进行抑制实验,发现MASP结合于MBL分子CLR中一个含16个氨基酸残基的区域,即成熟MBL肽链的第45～60位氨基酸残基,该区域位于Gly-X-Y三联体重复序列中Gly-Gln断裂的C端。还发现分别含1个突变残基的3种突变型(32Cys、34Asp和37Glu)MBL蛋白与MASP的结合具有类似野生型MBL蛋白的特征,但其结合能力明显降低,表明这3个突变残基位于MBL的MASP结合位点之外。
The detection system of human mannan-binding lectin (MBL) and MBL-associated serine protease (MASP) was established by ELISA. A series of corresponding short peptides of the CLL were designed and synthesized for inhibition experiment. MASP was found to bind to a region of 16 amino acid residues in the CLR of MBL molecule, that is, the amino acid residues 45-60 of the mature MBL peptide chain This region is located C-terminal to the Gly-Gln cleavage in the Gly-XY triplet repeat. Three mutant MBL proteins (32Cys, 34Asp and 37Glu) respectively containing MASK and one mutation were found to have similar characteristics of wild-type MBL protein, but their binding ability was significantly reduced, indicating that the three mutant residues Outside the MASP binding site of MBL.