Premium
A two‐dimensional electrophoretic profile for bacterial esterases
Author(s) -
Goullet Philippe,
Picard Bertrand
Publication year - 1985
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/elps.1150060307
Subject(s) - isoelectric focusing , esterase , electrophoresis , agarose , chromatography , chemistry , polyacrylamide gel electrophoresis , thin layer , biochemistry , enzyme , layer (electronics) , organic chemistry
Esterases produced by different bacterial species were separated by conventional electrophoresis (CE) in polyacrylamide agarose gel and by thin‐layer isoelectric focusing (IEF). Although CE revealed the greatest number of esterases and was preferable for their identification by specific hydrolytic activities, the two techniques appeared to be complementary in their resolving power for detection of electrophoretic variants. Consequently, by establishing a direct correspondence between homologous esterase bands resolved by CE and IEF, we have proposed a two‐dimensional electrophoretic profile (2‐DEP) which considerably refined the degree of esterase polymorphism and improved the enzymic differentiation between and within bacterial species.