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
USDA/Agronomy | 190 PABL; 1201 W. Gregory; Urbana, IL 61801
elarson at ux1.cso.uiuc.edu | Voice 217.244.3079 Fax 217.244.4419
Fidonet: 1:233/4.1 | My opinions are my own, but correct :-)
