首页> 外文期刊>Peptides: An International Journal >Isolation and characterization of a novel glutathione S-transferase-activating peptide from the oriental medicinal plant Phellodendron amurense.
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Isolation and characterization of a novel glutathione S-transferase-activating peptide from the oriental medicinal plant Phellodendron amurense.

机译:东方药用植物黄柏新谷胱甘肽S-转移酶激活肽的分离与鉴定。

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摘要

The aim of this study was to elucidate the characteristics of glutathione S-transferase (GST)-activating compounds from medicinal plants. Among 265 kinds of medicinal plants, Phellodendron amurense showed the highest GST activity at 174.8%. The GST-activating compound of P. amurense was maximally extracted when treated with distilled water at 30 degrees C for 12 h. The compound was purified by ultrafiltration, Sephadex G-10 gel filtration chromatography, and reverse-phase HPLC. The purified GST-activating compound from P. amurense was a novel tetrapeptide with an amino acid sequence of Ala-Pro-Trp-Cys and its molecular weight was estimated to be 476 Da. It also displayed a clear detoxicative effect in 1-chloro-2,4-dinitrobenzene treated mice at a dosage of mg/kg body weight.
机译:这项研究的目的是阐明药用植物中谷胱甘肽S转移酶(GST)激活化合物的特性。在265种药用植物中,黄柏的GST活性最高,为174.8%。当用蒸馏水在30°C下处理12 h时,最大程度地提取了黑松的GST活化化合物。通过超滤,Sephadex G-10凝胶过滤色谱和反相HPLC纯化化合物。纯化自A. amurense的GST活化化合物是一种新的四肽,其氨基酸序列为Ala-Pro-Trp-Cys,分子量估计为476 Da。在剂量为mg / kg体重的1-氯-2,4-二硝基苯处理的小鼠中,它还显示出明显的解毒作用。

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