Initiation Methionine of Recombinant Interleukin-2 is Completely Processed In Vivo by Replacement of the Second Proline Residue

概要

論文の詳細を見る
A portion of the recombinant interleukin-2 (rIL-2) produced in Escherichia coli had an amino (N-) terminal methionine. We found that this partial processing of the N-terminal methionine was caused by the proline residue, which is the second amino acid of IL-2. Alanine or histidine was substituted for proline by site-directid mutagenesis. There were no marked diferences between each mutein and rIL-2 in the amount of product, accumulation states or bioactivity. However, these muteins had no additional methionine at the amino terminus.
社団法人日本生物工学会の論文
1995-09-25