Characterization of Rat N-Acetylglucosaminyltransferase I Expressed in Esherichia coli
1995 年 59 巻 9 号 p. 1750-1752
詳細
1995 年 59 巻 9 号 p. 1750-1752
The catalytic domain (sGnT-I) of rat liver N-acetylglucosaminyl-transferase I (GnT-I) was expressed in Escherichia coli. Lysates from pETsGnT-I transformants contained a prominent protein species of 46kDa with which a significant GnT-I activity was associated. To purify the relevant enzyme, we constructed cDNAs encoding sGnT-ICH and sGnT-INH, which had six additional histi-dine residues as an affinity tag at the C-terminal and the N-terminal of sGnT-I, respectively, and introduced them into E. coli cells for expression. sGnT-INH was purified and its enzymatic properties were examined.
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