Apparent molecular weights of a heat-modifiable protein from the outer membrane of Escherichia coli in gels with different acrylamide concentrations.
AUTOR(ES)
Heller, K B
RESUMO
The apparent molecular weights of the two forms of a heat-modifiable protein from the outer membrane of Escherichia coli K-12, estimated in gels with different concentrations of acrylamide, indicate that the protein binds excess amounts of sodium dodecyl sulfate, possibly due to large beta structures before boiling.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=222370Documentos Relacionados
- Outer membrane of Serratia marcescens: apparent molecular weights of heat-modifiable proteins in gels with different acrylamide concentrations.
- Major heat-modifiable outer membrane protein in gram-negative bacteria: comparison with the ompA protein of Escherichia coli.
- Characterization of a heat-modifiable outer membrane protein of Haemophilus somnus.
- Metal ion dependence of a heat-modifiable protein from the outer membrane of Escherichia coli upon sodium dodecyl sulfate-gel electrophoresis.
- Variability of Low-Molecular-Weight, Heat-Modifiable Outer Membrane Proteins of Neisseria meningitidis