Recombinant production of enzymatically active male contraceptive drug target hTSSK2 - Localization of the TSKS domain phosphorylated by TSSK2
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- 作者：Jagathpala Shettya ; Rondedrick Sinvilleb ; Igor A. Shumilinc ; Wladek Minorc ; Jianhai Zhanga ; d ; Jon E. Hawkinsonb ; Gunda I. Georgb ; Charles J. Flickingera ; John C. Herra ; jch7k@virginia.edu" class="auth_mail" title="E-mail the corresponding author
- 关键词：TSSK2 ; Male contraceptive drug targets ; Recombinant kinases ; Mobility shift assay ; TSKS
- 刊名：Protein Expression and Purification
- 出版年：2016
- 出版时间：May 2016
- 年：2016
- 卷：121
- 期：Complete
- 页码：88-96
- 全文大小：1619 K
文摘
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Soluble full-length hTSSK2 was produced in a baculovirus expression system and purified.
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The biological activity of the recombinant hTSSK2 was studied by in vitro kinase and mobility shift assays.
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Recombinant hTSSK2 showed robust kinase activity in the in vitro kinase assay.
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The ATP Km values were similar for the highly and partially purified fractions of hTSSK2.
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In vitro phosphorylation experiments revealed that the N-terminus of hTSKS is phosphorylated by hTSSK2.