Premium
Nonspecific interactions alter lipopolysaccharide patterns and protein mobility on sodium dodecyl sulfate polyacrylamide gels
Author(s) -
Yuan Aidong,
Pardy Roosevelt L.,
Chia Catherine P.
Publication year - 1999
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/(sici)1522-2683(19990701)20:10<1946::aid-elps1946>3.0.co;2-y
Subject(s) - dithiothreitol , sodium dodecyl sulfate , esterase , chemistry , lipopolysaccharide , dictyostelium discoideum , bovine serum albumin , polyacrylamide , sodium , biochemistry , polyacrylamide gel electrophoresis , enzyme , incubation , albumin , substrate (aquarium) , gel electrophoresis , chromatography , biology , endocrinology , ecology , organic chemistry , gene , polymer chemistry
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.