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Abnormal SDS-PAGE migration of cytosolic proteins can identify domains and mechanisms that control surfactant binding

The amino acid substitution or post-translational modification of a cytosolic protein can cause unpredictable changes to its electrophoretic mobility during SDS-PAGE. This type of “gel shifting” has perplexed biochemists and biologists for decades. We identify a mechanism for “gel shifting” that pre...

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書誌詳細
主要な著者: Shi, Yunhua, Mowery, Richard A, Ashley, Jonathan, Hentz, Michelle, Ramirez, Alejandro J, Bilgicer, Basar, Slunt-Brown, Hilda, Borchelt, David R, Shaw, Bryan F
フォーマット: Artigo
言語:Inglês
出版事項: Wiley Subscription Services, Inc., A Wiley Company 2012
主題:
オンライン・アクセス:https://ncbi.nlm.nih.gov/pmc/articles/PMC3537240/
https://ncbi.nlm.nih.gov/pubmed/22692797
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.2107
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