UDP-glucose pyrophosphorylase is an important enzyme concerned with carbohydrate metabolism in plants. Cloning of UGPase is a premise for further study on molecular level, and it is also crucial for study of carbohydr...UDP-glucose pyrophosphorylase is an important enzyme concerned with carbohydrate metabolism in plants. Cloning of UGPase is a premise for further study on molecular level, and it is also crucial for study of carbohydrate metabolism. UGPase cDNA sequence as a template, designed primer, then 3'-untranslate region (3' UTR) of UGPase were amplified by 3'-rapid amplification of cDNA ends (3'-RACE). The results suggested the 3' UTR were 243 bp, contained AATAA sequence and Poly(A).展开更多
UGPase (UDP-glucose pyrophosphorylase), one of the primary enzymes concerned with carbohydrate metabolism, catalyzes the formation of UDPG. By inserting the UGPase cDNA fragment cloned from Saccharum officinarum int...UGPase (UDP-glucose pyrophosphorylase), one of the primary enzymes concerned with carbohydrate metabolism, catalyzes the formation of UDPG. By inserting the UGPase cDNA fragment cloned from Saccharum officinarum into PQE-30, the prokaryotic expression vector of PQE-UGP was successfully constructed. Then the vector plasmid of PQE-UGP was transformed into host bacteria M 15 and the expression of target gene was induced by Isopropyl β-D-1-Thiogalactopyranoside (IPTG). The research laid foundation for study on the prokaryotic expression of UGPase.展开更多
文摘UDP-glucose pyrophosphorylase is an important enzyme concerned with carbohydrate metabolism in plants. Cloning of UGPase is a premise for further study on molecular level, and it is also crucial for study of carbohydrate metabolism. UGPase cDNA sequence as a template, designed primer, then 3'-untranslate region (3' UTR) of UGPase were amplified by 3'-rapid amplification of cDNA ends (3'-RACE). The results suggested the 3' UTR were 243 bp, contained AATAA sequence and Poly(A).
文摘UGPase (UDP-glucose pyrophosphorylase), one of the primary enzymes concerned with carbohydrate metabolism, catalyzes the formation of UDPG. By inserting the UGPase cDNA fragment cloned from Saccharum officinarum into PQE-30, the prokaryotic expression vector of PQE-UGP was successfully constructed. Then the vector plasmid of PQE-UGP was transformed into host bacteria M 15 and the expression of target gene was induced by Isopropyl β-D-1-Thiogalactopyranoside (IPTG). The research laid foundation for study on the prokaryotic expression of UGPase.