Selective removal of N-terminal methionine from recombinant human growth hormone by an aminopeptidase isolated from Aspergillus flavus |
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Authors: | M-S Cho Y-P Lee H-S Chung |
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Affiliation: | (1) Dept Microbiology, Hannam University 133 Ojung-dong, Daeduk-ku, Taejon 300–791, Korea, KR;(2) Biotech Research Institute, LG Chem Research Park, Science Town, PO Box 61, Yu Sung, Taejon 305–380, Korea, KR |
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Abstract: | An aminopeptidase was isolated from a soil fungus, which specifically cleaves the unnatural N-terminal methionine in recombinant human growth hormone. Reaction mixtures with different ratios of aminopeptidase to recombinant methionyl human growth hormone showed that the removal of N-terminal methionine was complete at 1:200 (w/w), and more than 90% complete at ratios up to 1:2000 (w/w) when incubated for 24 h at 37°C. The data indicate that the aminopeptidase we have purified can be used for the efficient conversion of unnatural recombinant proteins to their natural form. Received 18 September 1997/ Accepted in revised form 17 April 1998 |
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Keywords: | : aminopeptidase N-terminal methionine recombinant protein recombinant human growth hormone |
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