Deoxynivalenol（DON） is a type B trichothecenes mycotoxin produced by several Fusarium species, often found in foodstuffs for humans and animals. DON is in great demand for the toxicological researches both in vivo a...Deoxynivalenol（DON） is a type B trichothecenes mycotoxin produced by several Fusarium species, often found in foodstuffs for humans and animals. DON is in great demand for the toxicological researches both in vivo and in vitro. In this work, wheat culture was inoculated with a Fusarium graminearum PH-1 strain for DON production. The solvent system for crude extraction was acetonitrile-water（84：16, v/v）. A simple two-step silica gel column chromatography was employed to separate the DON mycotoxin from wheat culture, combined with preparative high performance liquid chromatography（preparative HPLC） to purify the compound. The solvent system for the second silica gel column chromatography was methylene chloride-methanol（17：1, v/v）, which provided a good elution effect selected on thin layer chromatography（TLC）. The target compound was identified by HPLC, and the chemical structure was confirmed by mass spectrometry（MS） and ~1H and ^（13）C nuclear magnetic resonance（NMR） spectroscopy. A total of 433 mg of purified DON was obtained from 1 kg of wheat culture, with a purity of 99.01%. The study had provided an easy-operating and cost-effective method to isolate an expensive compound in a simple way.展开更多
A new way for the synthesis of human interferon—α_A monoclonal antibody (IFN-α_A-McAb) bound to silica gel packing material in high-performance affinity chromatography (HPAFC) has been developed. The high coupling ...A new way for the synthesis of human interferon—α_A monoclonal antibody (IFN-α_A-McAb) bound to silica gel packing material in high-performance affinity chromatography (HPAFC) has been developed. The high coupling efficiency and specific activity of IFN—α_A-McAb can be obtained by activated diol-silica gel with activating agent. After purification using this packing material in HPAFC, the specific activity of recombinant human interferon-α_A (rIFN-α_A) rose up to 1.03×10~7IU/mg protein and the purification efficiency is appoximately 100 times.展开更多
基金supported by the National Natural Science Foundation of China (31402268)the Natural Science Foundation of Jiangsu Province of China (BK20140691)+1 种基金Funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD), ChinaThe Introduction of International Advanced Agricultural Science and Technology Project from the Ministry of Agriculture of China (2012-Z22)
文摘Deoxynivalenol（DON） is a type B trichothecenes mycotoxin produced by several Fusarium species, often found in foodstuffs for humans and animals. DON is in great demand for the toxicological researches both in vivo and in vitro. In this work, wheat culture was inoculated with a Fusarium graminearum PH-1 strain for DON production. The solvent system for crude extraction was acetonitrile-water（84：16, v/v）. A simple two-step silica gel column chromatography was employed to separate the DON mycotoxin from wheat culture, combined with preparative high performance liquid chromatography（preparative HPLC） to purify the compound. The solvent system for the second silica gel column chromatography was methylene chloride-methanol（17：1, v/v）, which provided a good elution effect selected on thin layer chromatography（TLC）. The target compound was identified by HPLC, and the chemical structure was confirmed by mass spectrometry（MS） and ~1H and ^（13）C nuclear magnetic resonance（NMR） spectroscopy. A total of 433 mg of purified DON was obtained from 1 kg of wheat culture, with a purity of 99.01%. The study had provided an easy-operating and cost-effective method to isolate an expensive compound in a simple way.
文摘A new way for the synthesis of human interferon—α_A monoclonal antibody (IFN-α_A-McAb) bound to silica gel packing material in high-performance affinity chromatography (HPAFC) has been developed. The high coupling efficiency and specific activity of IFN—α_A-McAb can be obtained by activated diol-silica gel with activating agent. After purification using this packing material in HPAFC, the specific activity of recombinant human interferon-α_A (rIFN-α_A) rose up to 1.03×10~7IU/mg protein and the purification efficiency is appoximately 100 times.
