Heat modifiability and detergent solubility of outer membrane proteins of Rhodopseudomonas sphaeroides.
AUTOR(ES)
Kent, N E
RESUMO
The outer membrane fraction from Rhodopseudomonas sphaeroides was isolated by isopycnic density centrifugation. The purity of this fraction was assayed by several methods. When the outer membrane fraction obtained after French press lysis of cells was compared with the outer membrane fragments released during spheroplast formation, the polypeptide profiles were identical. Detergent solubilization of membrane fractions showed that Triton X-100 nonselectively solubilizes both the cytoplasmic membrane and the outer membrane, whereas Deriphat 160 selectively solubilizes the cytoplasmic membrane. Several outer membrane polypeptides, including the major outer membrane protein, exhibited changes in electrophoretic mobility that depended upon the temperature of solubilization in sodium dodecyl sulfate. Solubilization at room temperature in the presence of ions reproduced the effect of thermal denaturation on the major outer membrane polypeptide.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=217926Documentos Relacionados
- Effect of heat and 2-mercaptoethanol on intracytoplasmic membrane polypeptides of Rhodopseudomonas sphaeroides.
- Light-dependent regulation of the synthesis of soluble and intracytoplasmic membrane proteins of Rhodopseudomonas sphaeroides.
- Protein composition of Rhodopseudomonas sphaeroides outer membrane.
- Porin from Rhodopseudomonas sphaeroides.
- Intracellular localization of photosynthetic membrane growth initiation sites in Rhodopseudomonas sphaeroides.
