NDLI: Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels.

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Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels.

Content Provider	Semantic Scholar
Author	Yuan, Aidong Pardy, Rosevelt L. Chia, Catherine P.
Copyright Year	1999
Abstract	In testing whether bacterial lipopolysaccharide (LPS) was a natural substrate for an esterase from the soil amebae Dictyostelium discoideum, we observed altered banding patterns of the LPS and changed protein mobility on sodium dodecyl sulfate (SDS) polyacrylamide gels after incubation of LPS with the enzyme. The initial interpretation of these results was that the enzyme had removed ester-linked acyl chains from the LPS, leading to a change in its migration on gels. However, esterase inactivated by treatment with either dithiothreitol (DTT), heat, or SDS generated the same mobility shifts. Bovine serum albumin (BSA) also induced the same change in the electrophoretic pattern. We conclude that the altered LPS patterns and protein mobility on SDS gels were caused by nonspecific interactions between LPS and protein.
Starting Page	1
Ending Page	2
Page Count	2
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://digitalcommons.unl.edu/cgi/viewcontent.cgi?article=1072&context=bioscimicro
PubMed reference number	10451101v1
Volume Number	20
Issue Number	10
Journal	Electrophoresis
Language	English
Access Restriction	Open
Subject Keyword	Dithiothreitol Esterases Esters Lipopolysaccharides Polyacrylamide Gel Electrophoresis Serum Albumin Serum Albumin, Bovine Sodium Dodecyl Sulfate
Content Type	Text
Resource Type	Article

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