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Genetic polymorphism of apolipoprotein E: a variant form of apolipoprotein E2 distinguished by sodium dodecyl sulfate--polyacrylamide gel electrophoresis. by G Utermann; K H Weisgraber; W Weber; R W Mahley is a Medicine article available to read on EtoBox.

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T h e apolipoprotein E2 (apoE2) variant that possesses a cysteine substituted for an arginine at residue 158 in the amino acid sequence E2(Arg168 -+ Cys) can be distinguished by sodium dodecyl sulfate-polyacrylamide gel electrophoresis from other forms of apoE, including E3 (the parent form), E4(CyslI2 -Arg), E2(Arg14a "-\* Cys), and E ~( L Y S ~~~ -+ Gln). T h e E2(Argl,, -Cys) migrates as a distinctly separable band with a higher apparent molecular weight than the other forms. Chemical modification of apoE2(Argla8 -+ Cys) with sulfhydryl reagents (2-bromoethyl)-trimethylammonium bromide or cysteamine, which convert cysteine to arginyl or lysyl analogues, respectively, abolishes the difference in apparent molecular weight and results in the co-electrophoresis of E2(Argl5" -+ Cys) with other apoE forms. The mobilities of the other apoE variants are not affected by these modifications.llll9 These results suggest that the substitution site at residue 158 is a key location, important in modifying the behavior of apoE and in modulating its apparent molecular weight on sodium dodecyl sulfate-polyacrylamide gels. Furthermore, the technique used in this study may be very helpful in distin

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Author

G Utermann; K H Weisgraber; W Weber; R W Mahley

Publisher

Elsevier BV

Published

1984

Language

EN

Field

Medicine (Health Sciences)