The schizophyllan from Schizophyllum commune was purified and characterized. The crude schizo-phyllan was obtained from Schizophyllum commune fermentation broth by decoloration with activated carbon,followed by deprot...The schizophyllan from Schizophyllum commune was purified and characterized. The crude schizo-phyllan was obtained from Schizophyllum commune fermentation broth by decoloration with activated carbon,followed by deproteinization with Sevag method and ethanol precipitation. The pure schizophyllan was obtained by gel filtration chromatography with Sephacryl S-500,and its molecular characteristics were examined. The result showed that the molecular weight was 3.8×104 ,and the schizophyllan consisted of glucose with β-(1→6)-glucosidic linkages.展开更多
In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and d...In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and disposable polydimethylsiloxane （PDMS） using a silane-based chemical modification protocol, which yield antibody- terminated PDMS surfaces. In this study, the IX IP device is specifically designed for the purification of carbonylated protein, a representative example here to illustrate the potential applications for any other PTMs, which could be immuno-tagged by specific antibodies. The test model in vitro oxidized bovine serum albumin （BSA） was first derivitized by dinitrophenylhydrazide （DNPH） and then captured by the anti-DNP immobilized on this Ix lP device. The surface functional group mapping was systematically analyzed and validated by fluorescence microscopy. Quantitative study of DNP-derivatized carbonylated protein capture recovery and elution efficiency of the device was also studied. We also envision that this proteome enrichment Ix IP device can be assembled with other lab-on-a-chip components, such as microelectrophoresis or micro-chromatographic devices for follow-up protein analysis. This selective enrichment of modified proteins greatly facilitates the study of low abundant protein biomarkers discovery.展开更多
基金National Nature Science Foundation of China (No.31171662)"973"National Key Basic Research and Development Program(No.2012CB518202)+1 种基金Project of Qinghai Development of Science and Technology(No.2011-N-150)Key Project of GLD of PLA
文摘The schizophyllan from Schizophyllum commune was purified and characterized. The crude schizo-phyllan was obtained from Schizophyllum commune fermentation broth by decoloration with activated carbon,followed by deproteinization with Sevag method and ethanol precipitation. The pure schizophyllan was obtained by gel filtration chromatography with Sephacryl S-500,and its molecular characteristics were examined. The result showed that the molecular weight was 3.8×104 ,and the schizophyllan consisted of glucose with β-(1→6)-glucosidic linkages.
基金National Institutes of Health and the National Center for Research Resources grant number: P20RR01645 and NIH grant # DK44510
文摘In this paper, we report an antibody functionalized microimmunopreci- pitation （IX IP） method used for enrich lowabundant post-translational modified （PT~ proteins. The device is fabricated by inert, nontoxic and disposable polydimethylsiloxane （PDMS） using a silane-based chemical modification protocol, which yield antibody- terminated PDMS surfaces. In this study, the IX IP device is specifically designed for the purification of carbonylated protein, a representative example here to illustrate the potential applications for any other PTMs, which could be immuno-tagged by specific antibodies. The test model in vitro oxidized bovine serum albumin （BSA） was first derivitized by dinitrophenylhydrazide （DNPH） and then captured by the anti-DNP immobilized on this Ix lP device. The surface functional group mapping was systematically analyzed and validated by fluorescence microscopy. Quantitative study of DNP-derivatized carbonylated protein capture recovery and elution efficiency of the device was also studied. We also envision that this proteome enrichment Ix IP device can be assembled with other lab-on-a-chip components, such as microelectrophoresis or micro-chromatographic devices for follow-up protein analysis. This selective enrichment of modified proteins greatly facilitates the study of low abundant protein biomarkers discovery.
