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Autor:
Yi-Hang Lu, 盧逸航
94
Pigeon liver malic enzyme (EC. 1.1.1.40) is a homotetrameric enzyme. Each monomer contains 557 amino acid residues. The enzyme catalyzes oxidative decarboxylation of malate to pyruvate, requiring divalent metal ion with reduction of the coenz
Pigeon liver malic enzyme (EC. 1.1.1.40) is a homotetrameric enzyme. Each monomer contains 557 amino acid residues. The enzyme catalyzes oxidative decarboxylation of malate to pyruvate, requiring divalent metal ion with reduction of the coenz
Externí odkaz:
http://ndltd.ncl.edu.tw/handle/36250925418217533035
Autor:
Lan Li, Jie-hong Yang, Chang Li, Hui-fen Zhou, Li Yu, Xiao-long Wu, Yi-hang Lu, Yu He, Hai-tong Wan
Publikováno v:
Biomedicine & Pharmacotherapy. 163:114887
Autor:
Jing-De Zhao, Yi-Hang Lu
Publikováno v:
Energy and Mechanical Engineering.
Autor:
Hui Chuan Chang, Gu-Gang Chang, Yi Hang Lu, Meng Ying Li, Yu Hou Chen, Chao Hsiung Lin, Liang Yu Chen
Malic enzyme is a tetrameric protein with double dimer quaternary structure. In 3-5 M urea, the pigeon cytosolic NADP(+)-dependent malic enzyme unfolded and aggregated into various forms with dimers as the basic unit. Under the same denaturing condit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d758bb327d29419f289a14c0209ac9ad
https://europepmc.org/articles/PMC2084232/
https://europepmc.org/articles/PMC2084232/
Autor:
Yi-Hang Lu, Jing-De Zhao
Publikováno v:
Energy & Mechanical Engineering - Proceedings of 2015 International Conference; 2016, p371-377, 7p