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人嗜铬颗粒蛋白A(CgA)是存在于许多神经内分泌细胞和内分泌细胞的分泌颗粒内的酸性蛋白质.我们通过CgA多抗、单抗和人CgA合成多肽间的结合反应研究人CgA的线性抗原位点,结果表明合成多肽CgA1-20、47-67、107-158、254-297、331-375、395-439和CgA25-46、163-210、231-253、298-314呈现无抗原性或弱抗原性.而合成多肽CgA68-106、222-230、315-330和376-394则呈现强抗原性.两株人CgA鼠源单抗B4E11和A11识别的氨基酸残基分别为CgA68-70(GAK)、CgA81-90(GFEDELSEVL).我们的研究将有助于选择针对CgA片段特异性的抗体,而这些抗体则可应用于CgA分子的结构和功能的研究,或提供对CgA阳性的内分泌和神经内分泌肿瘤进行体内外诊断的新方法.
Human Chromogranin A (CgA) is an acidic protein present in secretory granules of many neuroendocrine cells and endocrine cells.We studied the linear antigen of human CgA by the binding reaction between CgA polyclonal, monoclonal antibody and human CgA synthetic polypeptide The results showed that the synthetic peptides CgA1-20, 47-67, 107-158, 254-297, 331-375, 395-439 and CgA25-46, 163-210, 231-253, 298-314 showed no antigenicity Or weak antigenicity, whereas the synthetic peptides CgA68-106, 222-230, 315-330 and 376-394 showed strong antigenicity.The amino acid residues recognized by the two human CgA murine monoclonal antibodies B4E11 and A11 were CgA68-70 (GAK), CgA81-90 (GFEDELSEVL) Our study will help to select antibodies specific for CgA fragments that can be applied to the study of the structure and function of CgA molecules or to CgA-positive endocrine And neuroendocrine tumors in vitro and in vivo diagnostic methods.