利用ＰＣＲ技术并进行ＤＮＡ序列测定，从人脑ｃＤＮＡ库中扩增得到人豆蔻酰ＣｏＡ∶蛋白质Ｎ端豆蔻酰转移酶（ｈＮＭＴ）的编码基因，构建其在Ｔ７启动子控制下的成熟型和Ｈｉｓ６融合型的表达质粒ｐＭＦｈＮＭＴ３和ｐＭＦＨＴｈＮＭＴ２，转化大肠杆菌ＢＬ２１（ＤＥ３），进行ＩＰＴＧ诱导表达研究。ＳＤＳ－ＰＡＧＥ分析结果显示，在３７℃条件下表达的各种重组ｈＮＭＴ几乎全是不溶性产物，但在较低温度（２２℃）条件下表达的Ｈｉｓ６ｈＮＭＴ绝大部分为可溶性产物，约占细菌可溶性总蛋白的７％左右。利用固定化金属离子（Ｎｉ２＋）配体亲和层析，从表达菌的可溶性总蛋白中一步纯化目的蛋白，纯度达８０％以上。体外标记测定酶活力的实验结果表明，上述表达并纯化的Ｈｉｓ６－ｈＮＭＴ具有催化豆蔻酰基转移的活力。 The gene encoding myristoyl CoA: protein N-terminal myristoyltransferase (hNMT) was amplified from the human brain cDNA library by PCR and DNA sequencing to construct its mature type and His6 under the control of the T7 promoter Fusion expression plasmid pMF  hNMT3 and pMFHT  hNMT2, transformed into E. coli BL21 (DE3), IPTG induced expression studies. SDS-PAGE analysis showed that all recombinant hNMTs expressed at 37 ℃ were almost insoluble products, but most of His6-hNMT expressed at lower temperature (22 ℃) were soluble products, accounting for about bacteria About 7% of total soluble protein. Purification of the target protein from the total soluble total protein of the expressed bacteria was carried out with the immobilized metal ion (Ni2 +) ligand affinity chromatography at a purity of over 80%. The results of in vitro assay of enzyme activity showed that His6-hNMT expressed and purified as described above has the activity of catalyzing myristoyl transfer.