6H-SiC is an important semiconductor material. The 6H-SiC wafer is always exposed to a high-humidity environment and the effect from the absorbed water molecule and some relative adsorbates is not negligible. Here, th...6H-SiC is an important semiconductor material. The 6H-SiC wafer is always exposed to a high-humidity environment and the effect from the absorbed water molecule and some relative adsorbates is not negligible. Here, the oxygen and water molecules absorbed on the 6H-SiC(0001) surface and the dissociation process were studied with density functional theory. On the 6H-SiC(0001) surface, absorbed O2 is spontaneously dissociated into O*, which is absorbed on a hollow site, and further transforms the 6H-SiC(0001) surface into SiO2. The absorbed H2O is spontaneously broken into OH*and H*, which are both absorbed on the top of the Si atom, and OH* is further reversibly transformed into O* and H*. The H* could saturate the dangling Si bond and change the absorption type of O*, which could stabilize the 6H-SiC(0001) surface and prevent it from transforming into SiO2.展开更多
Midkine is a heparin-binding growth factor, which plays important roles in the regulation of cell growth and differentiation. The non-tagged recombinant human midkine （rhMK） is therefore required to facilitate its f...Midkine is a heparin-binding growth factor, which plays important roles in the regulation of cell growth and differentiation. The non-tagged recombinant human midkine （rhMK） is therefore required to facilitate its functional studies of this important growth factor. In the present work, rhMK was expressed in Escherichia coli （E. coli） BL21 （DE3）. The expression of midkine was efficiently induced by isopropyl-13-D-thiogalactopyranoside （IPTG）. After sonication, midkine was recovered in an insoluble form, and was dissolved in guanidine hydrochloride buffer. Renaturation of the denatured protein was carried out in the defined protein refolding buffer, and the refolded protein was purified using S-Sepharose ion-exchange chromatography. The final preparation of the rhMK was greater than 98% pure as measured by sodium dodecylsulfate-polyacrylamid gel electrophoresis （SDS-PAGE） and reverse phase high performance liquid chromatography （RP-HPLC）. The purified rhMK enhanced the proliferation of NIH3T3 cells.展开更多
基金supported by the Fundamental Research Project of Qinghai Province (2017-ZJ-795)
文摘6H-SiC is an important semiconductor material. The 6H-SiC wafer is always exposed to a high-humidity environment and the effect from the absorbed water molecule and some relative adsorbates is not negligible. Here, the oxygen and water molecules absorbed on the 6H-SiC(0001) surface and the dissociation process were studied with density functional theory. On the 6H-SiC(0001) surface, absorbed O2 is spontaneously dissociated into O*, which is absorbed on a hollow site, and further transforms the 6H-SiC(0001) surface into SiO2. The absorbed H2O is spontaneously broken into OH*and H*, which are both absorbed on the top of the Si atom, and OH* is further reversibly transformed into O* and H*. The H* could saturate the dangling Si bond and change the absorption type of O*, which could stabilize the 6H-SiC(0001) surface and prevent it from transforming into SiO2.
基金Project supported in part by the Hi-Tech Research and Development Program(863) of China(No.2007AA02Z149)the Science and Technology Commissionof Shanghai Municipality(No.075407071),China
文摘Midkine is a heparin-binding growth factor, which plays important roles in the regulation of cell growth and differentiation. The non-tagged recombinant human midkine （rhMK） is therefore required to facilitate its functional studies of this important growth factor. In the present work, rhMK was expressed in Escherichia coli （E. coli） BL21 （DE3）. The expression of midkine was efficiently induced by isopropyl-13-D-thiogalactopyranoside （IPTG）. After sonication, midkine was recovered in an insoluble form, and was dissolved in guanidine hydrochloride buffer. Renaturation of the denatured protein was carried out in the defined protein refolding buffer, and the refolded protein was purified using S-Sepharose ion-exchange chromatography. The final preparation of the rhMK was greater than 98% pure as measured by sodium dodecylsulfate-polyacrylamid gel electrophoresis （SDS-PAGE） and reverse phase high performance liquid chromatography （RP-HPLC）. The purified rhMK enhanced the proliferation of NIH3T3 cells.
