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Shibata, Hitoshi,Tanaka, Tomoyuki,Yonemura, Takeshi,Sawa, Yoshihiro,Ishikawa, Takahiro Korean Society of Photoscience 2002 Journal of Photosciences Vol.9 No.2
Since solar radiation contains wavelength essential for photosynthesis accompanying with near-UV light, UV-B effects on biological parameters and acclimation mechanisms are influenced by photosynthetically active radiation (PAR). Therefore, to elucidate near-UV shielding mechanism in higher plants, we cultivated cauliflower under usual solar radiation and increased UV-B from fluorescent lamps, two- or three-fold excess over continuously estimated UV-B dose in PAR during daytime, using computer regulated systems. Increased UV-B radiation had little effect on growth expressed as fresh weigh and leaf area. Water soluble low molecular weight compounds showing absorption in near UV region were enhanced according to the irradiated UV-B dose. One of compounds in cauliflower leaves was identified as chlorogenic acid. This was found to have no near-UV photosenSitizerable activity and is known to have an ability to scavenge a wide species of active oxygen. Another pro-oxidant compound that generates superoxide anion radical under near-UV irradiation was not induced by increased UV-B during cultivation, and identified as lumazine, a degradation product from folic acid.
Azad, Md. Abul Kalam,Sawa, Yoshihiro,Ishikawa, Takahiro,Shibata, Hitoshi Korean Society for Biochemistry and Molecular Biol 2006 Journal of biochemistry and molecular biology Vol.39 No.6
The holoenzyme of protein phosphatase (PP) from tulip petals was purified by using hydrophobic interaction, anion exchange and microcystin affinity chromatography to analyze activity towards p-nitrophenyl phosphate (p-NPP). The catalytic subunit of PP was released from its endogenous regulatory subunits by ethanol precipitation and further purified. Both preparations were characterized by immunological and biochemical approaches to be PP2A. On SDS-PAGE, the final purified holoenzyme preparation showed three protein bands estimated at 38, 65, and 75 kDa while the free catalytic subunit preparation showed only the 38 kDa protein. In both preparations, the 38 kDa protein was identified immunologically as the catalytic subunit of PP2A by using a monoclonal antibody against the PP2A catalytic subunit. The final 623- and 748-fold purified holoenzyme and the free catalytic preparations, respectively, exhibited high sensitivity to inhibition by 1 nM okadaic acid when activity was measured with p-NPP. The holoenzyme displayed higher stimulation in the presence of ammonium sulfate than the free catalytic subunit did by protamine, thereby suggesting different enzymatic behaviors.
( Abul Kalam Azad ),( Asraful Jahan ),( Mahbub Hasan ),( Takahiro Ishikawa ),( Yoshihiro Sawa ),( Hitoshi Shibata ) 생화학분자생물학회(구 한국생화학분자생물학회) 2011 BMB Reports Vol.44 No.11
The Sec61α subunit is the core subunit of the protein conducting channel which is required for protein translocation in eukaryotes and prokaryotes. In this study, we cloned a Sec61α subunit from Penicillium ochrochloron (PoSec61α). Sequence and 3D structural model analysis showed that PoSec61α conserved the typical characteristics of eukaryotic and prokaryotic Sec61α subunit homologues. The pore ring known as the constriction point of the channel is formed by seven hydrophobic amino acids. Two methionine residues from transmembrane α-helice 7 (TM7) contribute to the pore ring formation and projected notably to the pore area and narrowed the pore compared with the superposed residues at the corresponding positions in the crystal structures or the 3D models of the Sec61α subunit homologues in archaea or other eukaryotes, respectively. Results reported herein indicate that the pore ring residues differ among Sec61α subunit homologues and two hydrophobic residues in the TM7 contribute to the pore ring formation. [BMB reports 2011; 44(11): 719-724]