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首页> 外文期刊>Journal of Bioscience and Bioengineering >Production and Characterization of Active Soluble Human #beta#1,4-Galactosyltransferase in Escherichia coli as a Useful Catalyst in Synthesis of the Gal #beta#beta#(->)4 GlcNAc Linkage
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Production and Characterization of Active Soluble Human #beta#1,4-Galactosyltransferase in Escherichia coli as a Useful Catalyst in Synthesis of the Gal #beta#beta#(->)4 GlcNAc Linkage

机译:活性可溶性人#beta#1,4-半乳糖基转移酶在大肠杆菌中的生产和表征,可作为合成Gal#beta#beta#(->)4 GlcNAc连锁反应的有用催化剂

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摘要

An active and sluble human #beta#1,4-galactosyltransferase(#beta#-GT) was produced in Escherichia coli using a maltose-binding protein fusion system.The purified recombiant #beta#-GT has a K_m value of 0.035mM for UDP-galactose and a V_(max) of 643X10~3nmol/mg/h.The enzyme catalyzes the transfer of galactose from UDP-galactose to N-linked oligosaccharides.The properties of the purified enzyme were identical to those of bovine milk #beta#-GT.
机译:使用麦芽糖结合蛋白融合系统在大肠杆菌中生产了一种活性且可溶性的人#beta#1,4-半乳糖基转移酶(#beta#-GT)。纯化的重组蛋白#beta#-GT的K_m值为0.035mM UDP-半乳糖和V_(max)为643X10〜3nmol / mg / h。该酶催化将半乳糖从UDP-半乳糖转移至N-连接的寡糖,纯化后的酶的性质与#beta牛乳相同#-GT

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