초록
<P><B>Highlights</B></P><P>► The monomeric insulin B27 DTrI precursor (MIP) was prepared by intein mediated expression in <I>Escherichia coli</I>. ► The B27K-DTrI insulin was obtained by tryptic digestion, further purified by HPLC and analyzed by mass spectrometry. ► The molecular mass of purified B27K-DTrI was consistent with the theoretical value.</P> <P><B>Abstract</B></P><P>The B27K-DTrI insulin (human insulin with B28–30 removed and B27 Thr replaced by Lys) was reported to have superior monomeric property with 80% insulin activity <I>in vivo</I>. It has potential use as a new fast-acting analog of insulin. We cloned the monomeric insulin B27 DTrI precursor (MIP) into the pTWIN1 vector, and prepared by intein mediated expression in <I>Escherichia coli</I>. After tryptic digestion, the MIP was converted to B27K-DTrI insulin. The product was purified by HPLC. The mass spectrometry showed that the molecular mass of purified B27K-DTrI was consistent with the theoretical value.</P>