tris-glycine vs tricine

larson eric elarson at ux1.cso.uiuc.edu
Tue Jan 10 10:21:51 EST 1995


pnh at fcsparc6.ncifcrf.gov (Paul N Hengen) writes:

>| Does anyone know what are the advantages/disadvantages of tris-glycine 
>| vs. tricine gels for electrophoresis of proteins?

>The use of tricine allows resolution of proteins in the < 5,000 Dalton
>range better than glycine. Also, the proteins may be recovered for
>microsequencing without modification problems.

>author = "H. {Sch\"{a}gger}
>     and G. von Jagow",
>title = "Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis
>for the separation of proteins in the range from 1 to 100 {kDa}",
>journal = "Anal. Biochem.",
>volume = "166",
>pages = "368-379",
>year = "1987"}
=========
 
Okajima, T., T. Tanage, and T. Yasuda (1993) Anal. Biochem 211: 293-300
 
Has a procedure adapted from Laemmli that allows for small mol. wt. peptide
separation.  The technique works (though I had to change to 16% gels from
the 20% the authors used.)  Basically, it's a Laemmli gel with 2X higher
concentrations of buffer in stacking and running gel.  This makes the
procedure "simple" in that two sets of buffer stocks don't need to be
around.  I haven't tried the gels with normal proteins (because the %
acrylamide is too high.)

-- 
Eric Larson                  | University of Illinois at Urbana-Champaign
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