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- jbb.99.303 date "2005-04-01".
- jbb.99.303 doi "10.1263/jbb.99.303".
- jbb.99.303 first "Surinder Mohan".
- jbb.99.303 first2 "Amulya Kumar".
- jbb.99.303 isCitedBy Inclusion_bodies.
- jbb.99.303 issue "4".
- jbb.99.303 journal "Journal of Bioscience and Bioengineering".
- jbb.99.303 last "Singh".
- jbb.99.303 last2 "Panda".
- jbb.99.303 pages "303–310".
- jbb.99.303 pmid "16233795".
- jbb.99.303 quote "Inclusion bodies are dense electron-refractile particles of aggregated protein found in both the cytoplasmic and periplasmic spaces of E. coli during high-level expression of heterologous protein. It is generally assumed that high level expression of non-native protein and highly hydrophobic protein is more prone to lead to accumulation as inclusion bodies in E. coli. In the case of proteins having disulfide bonds, formation of protein aggregates as inclusion bodies is anticipated since the reducing environment of bacterial cytosol inhibits the formation of disulfide bonds. The diameter of spherical bacterial inclusion bodies varies from 0.5–1.3 μm and the protein aggregates have either an amorphous or paracrystalline nature depending on the localization. Inclusion bodies have higher density than many of the cellular components, and thus can be easily separated by high-speed centrifugation after cell disruption. Inclusion bodies despite being dense particles are highly hydrated and have a porous architecture.".
- jbb.99.303 subscription "Yes".
- jbb.99.303 title "Solubilization and refolding of bacterial inclusion body proteins".
- jbb.99.303 url "http://www.sciencedirect.com/science/article/pii/S1389172305703728".
- jbb.99.303 volume "99".