排序方式: 共有5条查询结果,搜索用时 15 毫秒
1
1.
2.
3.
Pakorn Bovonsombat Rameez Ali Chiraphorn Khan Juthamard Leykajarakul Kawin Pla-on Suraj Aphimanchindakul Natchapon Pungcharoenpong Nisit Timsuea Anchalee Arunrat Napat Punpongjareorn 《Tetrahedron》2010,66(34):6928-181
para-Regioselective bromination of phenol and analogues, promoted by p-toluenesulfonic acid, is achieved in high to excellent yields at room temperature with N-bromosuccinimide. Chlorination with N-chlorosuccinimide and catalysed by p-toluenesulfonic acid also gives para-chlorinated phenol analogues in good yields at room temperature. 相似文献
4.
Thongboonkerd V Songtawee N Kanlaya R Chutipongtanate S 《Analytical and bioanalytical chemistry》2006,384(4):964-971
There is a need for a simple method that can directly quantify hydrophobic proteins. UV-visible spectrophotometry was applied
in the present study for this purpose. Absorbance at λ=280 nm (A
280) was detected for both Escherichia coli membrane proteins and bovine serum albumin, whereas absorbance at λ=620 nm (A
620) was only detected for E. coli membrane proteins. The A
620 values of the brain samples were greater than those of heart samples when equal concentrations were used, regardless of the
type of solubilizing agent employed. Because hydrophobic proteins tend to form colloidal microparticles in solution, we also
applied UV-visible spectrophotometry to evaluate the efficacies of different extraction protocols for solubilizing hydrophobic
proteins. For brain protein extraction, the highest A
620 was observed in samples recovered using Tris, whereas the lowest was from samples recovered using SDS. Solubilizing brain
tissue with 0.25% SDS (above the CMC) gave a lower A
620 than extraction with 0.025% SDS (below the CMC). Addition of 0.25% SDS to samples recovered with Triton caused A
620 to drop. A
620 could also be used to distinguish between the hydrophobic fractions (pellets) of brain and urine proteins and their hydrophilic
fractions (supernatants) prefractionated using high-speed centrifugation. Additionally, an A
620/A
280 ratio exceeding 0.12 appears to denote highly hydrophobic samples. Our data suggest that direct UV-visible spectrophotometry
can be used as a simple method to quantify and evaluate the solubilities of hydrophobic proteins. 相似文献
5.
Illuminating the origins of spectral properties of green fluorescent proteins via proteochemometric and molecular modeling 下载免费PDF全文
1