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Ru-ren Li,Qun-li Yu,Ling Han,Liang-yan Rong,Meng-meng Yang,Mai-rui An 한국화학공학회 2014 Korean Journal of Chemical Engineering Vol.31 No.11
A novel hyaluronidase (BgHya1) from Yak testis was isolated and shown to have compara-tively high activity on sodium hyaluronate. However, surveys on BgHya1 are still limited. The enzyme was purifiedthrough gel filtration on Sephacryl S-100 and cation-exchange on SP Sepharose fast flow; the purity was confirmedby a reverse phase FPLC Shodex C4 column. The specific activity of the purified BgHya1 was 20.4 U/mg assayed bythe colorimetric method against 0.85 U/mg for the crude enzyme, representing a 24-fold purification. It was a monomericprotein of 55 kDa estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and SephacrylS-200. It exhibited maximum activity in the presence of 0.15 M NaCl at 37 oC, pH 3.8, and a specificity to sodiumhyaluronate higher than that of chondroitin-4-sulfate, chondroitin-6-sulfate, and dermatan. The Km value for BgHya1,using sodium hyaluronate as substrate, was 0.106 mg/mL. Activity of BgHya1 was inhibited mildly by Ca2+and Fe2+,and significantly by Fe3+, Mg2+, EDTA, urea, heparin, and 0.5 M NaCl. It was not affected by Cu2+,Zn2+,Co2+, ascorbicacid, PMSF, DTT, glutathione (reduced), or L-cysteine. BgHya1 was shown to be heat unstable in the range of 4-45 oC. In terms of storage stability, 92% of the activity was retained after four weeks at 4 oC, and 58% at room temperature. In addition, adding BSA (1.0 mg/mL) to the enzyme sample prior to freezing resulted in complete retention of enzymeactivity. This work yielded a high purity hyaluronidase, the first one isolated from by-product.
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Impact of a Glyphosate-Tolerant Soybean Line on the Rhizobacteria, Revealed by Illumina MiSeq
( Gui-hua Lu ),( Yin-ling Zhu ),( Ling-ru Kong ),( Jing Cheng ),( Cheng-yi Tang ),( Xiao-mei Hua ),( Fan-fan Meng ),( Yan-jun Pang ),( Rong-wu Yang ),( Jin-liang Qi ),( Yong-hua Yang ) 한국미생물 · 생명공학회 2017 Journal of microbiology and biotechnology Vol.27 No.3
The global commercial cultivation of transgenic crops, including glyphosate-tolerant soybean, has increased widely in recent decades with potential impact on the environment. The bulk of previous studies showed different results on the effects of the release of transgenic plants on the soil microbial community, especially rhizosphere bacteria. In this study, comparative analyses of the bacterial communities in the rhizosphere soils and surrounding soils were performed between the glyphosate-tolerant soybean line NZL06-698 (or simply N698), containing a glyphosate-insensitive EPSPS gene, and its control cultivar Mengdou12 (or simply MD12), by a 16S ribosomal RNA gene (16S rDNA) amplicon sequencing-based Illumina MiSeq platform. No statistically significant difference was found in the overall alpha diversity of the rhizosphere bacterial communities, although the species richness and evenness of the bacteria increased in the rhizosphere of N698 compared with that of MD12. Some influence on phylogenetic diversity of the rhizosphere bacterial communities was found between N698 and MD12 by beta diversity analysis based on weighted UniFrac distance. Furthermore, the relative abundances of part rhizosphere bacterial phyla and genera, which included some nitrogen-fixing bacteria, were significantly different between N698 and MD12. Our present results indicate some impact of the glyphosate-tolerant soybean line N698 on the phylogenetic diversity of rhizosphere bacterial communities together with a significant difference in the relative abundances of part rhizosphere bacteria at different classification levels as compared with its control cultivar MD12, when a comparative analysis of surrounding soils between N698 and MD12 was used as a systematic contrast study.
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Diabetes Promotes Myocardial Fibrosis via AMPK/EZH2/PPAR-γ Signaling Pathway
Shan-Shan Li,Lu Pan,Zhen-Ye Zhang,Meng-Dan Zhou,Xu-Fei Chen,Ling-Ling Qian,Min Dai,Juan Lu,Zhi-Ming Yu,Shipeng Dang,Ru-Xing Wang 대한당뇨병학회 2024 Diabetes and Metabolism Journal Vol.48 No.4
Background: Diabetes-induced cardiac fibrosis is one of the main mechanisms of diabetic cardiomyopathy. As a common histone methyltransferase, enhancer of zeste homolog 2 (EZH2) has been implicated in fibrosis progression in multiple organs. However, the mechanism of EZH2 in diabetic myocardial fibrosis has not been clarified.Methods: In the current study, rat and mouse diabetic model were established, the left ventricular function of rat and mouse were evaluated by echocardiography and the fibrosis of rat ventricle was evaluated by Masson staining. Primary rat ventricular fibroblasts were cultured and stimulated with high glucose (HG) <i>in vitro</i>. The expression of histone H3 lysine 27 (H3K27) trimethylation, EZH2, and myocardial fibrosis proteins were assayed.Results: In STZ-induced diabetic ventricular tissues and HG-induced primary ventricular fibroblasts in vitro, H3K27 trimethylation was increased and the phosphorylation of EZH2 was reduced. Inhibition of EZH2 with GSK126 suppressed the activation, differentiation, and migration of cardiac fibroblasts as well as the overexpression of the fibrotic proteins induced by HG. Mechanical study demonstrated that HG reduced phosphorylation of EZH2 on Thr311 by inactivating AMP-activated protein kinase (AMPK), which transcriptionally inhibited peroxisome proliferator-activated receptor γ (PPAR-γ) expression to promote the fibroblasts activation and differentiation.Conclusion: Our data revealed an AMPK/EZH2/PPAR-γ signal pathway is involved in HG-induced cardiac fibrosis.
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