Tetramer-organizing polyproline-rich peptides differ in CHO cell-expressed and plasma-derived human butyrylcholinesterase tetramers
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- 作者：Lawrence M. Schopfer ; lmschopf@unmc.edu" class="auth_mail" title="E-mail the corresponding author ; Oksana Lockridge olockrid@unmc.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：rBChE ; recombinant butyrylcholinesterase ; MALDI TOF ; matrix-assisted laser desorption&ndash ; ionization time-of-flight ; CHO ; Chinese hamster ovary ; ATCC ; American Type Culture Collection ; AChE ; acetylcholinesterase ; NCBI ; National Center for Biotechnology Information ; BLASTp ; Basic Local Alignment Search Tool for proteins from NCBI ; NCBInr ; National Center for Biotechnology Information non-redundant protein database ; ColQ ; a collagenous protein membrane anchor ; PRiMA ; proline-rich membrane anchor
- 刊名：Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
- 出版年：2016
- 出版时间：June 2016
- 年：2016
- 卷：1864
- 期：6
- 页码：706-714
- 全文大小：2853 K
文摘
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Polyproline-rich peptides organize human butyrylcholinesterase tetramers.
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Tetramer-organizing peptides in CHO cells differ from those in plasma.
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70% of tetramer-organizing peptides in plasma come from lamellipodin.
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60 proteins contribute tetramer-organizing peptides in CHO cells.