| Literature DB >> 350841 |
Abstract
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.Entities:
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Year: 1978 PMID: 350841 PMCID: PMC222370 DOI: 10.1128/jb.134.3.1181-1183.1978
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490