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Isolation and characterization of recombinant Drosophila Copia aspartic proteinase

The wild type Copia Gag precursor protein of Drosophila melanogaster expressed in Escherichia coli was shown to be processed autocatalytically to generate two daughter proteins with molecular masses of 33 and 23 kDa on SDS/PAGE. The active-site motif of aspartic proteinases, Asp-Ser-Gly, was present...

詳細記述

保存先:
書誌詳細
主要な著者: Athauda, Senarath B. P., Yoshioka, Katsuji, Shiba, Tadayoshi, Takahashi, Kenji
フォーマット: Artigo
言語:Inglês
出版事項: Portland Press Ltd. 2006
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC1615899/
https://ncbi.nlm.nih.gov/pubmed/16813567
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20060800
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