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从人甲状旁腺瘤组织中分离到ｍＲＮＡ，逆转成ｃＤＮＡ后，设计带有突变碱基的引物，通过聚合酶链式反应，扩增ｈＰＴＨ基因，使Ｎ端前５氨基酸的碱基富含腺嘌呤核苷（Ａ）．将该基因克隆到表达载体ＰＥＴＩＣ上，转化大肠杆菌ＢＬ２１（ＤＥ３）表达，实验证实ｈＰＴＨ的表达量占菌体蛋白总量的１１％；细胞粗步处理产物经腺苷环化酶的生物鉴定实验证实，重组ｈＰＴＨ具有生物活性，粗产物５００倍稀释后，ｈＰＴＨ的放免活性为２０６．５ｎｇ／Ｌ，为对照的４１５倍
MRNA was isolated from human parathyroid tumor tissue, and after reversal into cDNA, primers with a mutated base were designed to amplify the hPTH gene by polymerase chain reaction so that the base of the first 5 amino acids of N-terminal was rich in gland Purine nucleoside (A). The gene was cloned into the expression vector PETIC and transformed into E. coli BL21 (DE3). The expression of hPTH was confirmed to account for 11% of the total bacterial proteins. The crude cell-treated cells were identified by adenylyl cyclase Confirmed that the recombinant hPTH has biological activity, crude 500-fold diluted, hPTH radioactivity was 206.5ng / L, 415 times the control