A highly stable cambialistic-superoxide dismutase from Antrodia camphorata: expression in yeast and enzyme properties.
作者： Yi-Jen Liau , Lisa Wen , Jei-Fu Shaw , Chi-Tsai Lin
DOI: 10.1016/J.JBIOTEC.2007.05.021
关键词: Complementary DNA 、 Superoxide dismutase 、 Homology (biology) 、 Protein subunit 、 Molecular biology 、 Dimer 、 Chemistry 、 Antrodia 、 Biochemistry 、 Enzyme 、 Yeast
摘要: Abstract A cDNA encoding a putative superoxide dismutase (SOD) was identified in expressed sequence tags of Antrodia camphorata, medicinal mushroom found only Taiwan. The deduced protein aligned with Mn-SODs and Fe-SODs from other organisms, this SOD showed greater homology to Mn-SOD. Functional A. camphorata overexpressed yeast purified. purified enzyme two active forms on 12.5% native PAGE, dimer monomer. dimeric protein's half-life deactivation at 80 °C 7 min, its thermal inactivation rate constant Kd 9.87 × 10−2 min−1. stable broad pH range 5–11; the presence 0.4 M imidazole 2% SDS. atomic absorption spectrometric assay that 1.0 atom manganese/iron (9:1) present each subunit. high stability make it better suited than cambialistic-SODs for use cosmetics. also documents future utility developing anti-inflammatory agent treatment chronic diseases.
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