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Separation of serum cholinesterase molecular forms from three rodent species by gradient polyacrylamide gel electrophoresis
Author(s) -
Bisso Guillermo M.
Publication year - 1986
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.1150070512
Subject(s) - acetylthiocholine , cholinesterase , polyacrylamide gel electrophoresis , chemistry , electrophoresis , chromatography , polyacrylamide , biochemistry , gel electrophoresis , acetylcholinesterase , biology , enzyme , microbiology and biotechnology , aché , pharmacology
Gradient (5–30 %) polyacrylamide gel electrophoresis (PAGE) was used for the analysis of serum cholinesterases from the spiny mouse, the mouse and the rat. Enzymatic staining of slab gels was performed using acetylthiocholine as substrate. Eserine, 1.5‐bis(4‐allyldimethylammoniumphenyl)‐pentane‐3‐one dibromide (BW284C51) and tetraisopropylpyrophosphoramide (iso‐OMPA) were used as selective specific inhibitors of total, true and pseudo‐cholinesterase, respectively. Five main molecular forms were detected in the three species as sharp, well separated bands. All bands were inhibited completely by eserine while the effects of BW 284C51 and iso‐OMPA varied in the three species. This result suggests a common qualitative pattern for the three rodents with a different distribution of true and pseudo‐cholinesterase molecular forms for each species. The good resolution shown by the reported densitometric scan recordings confirms the advantages of gradient over homogeneous PAGE in the study of serum cholinesterases.