A new siliconized-glass fiber as support for protein-chemical analysis of electroblotted proteins.
A new hydrophobic glass-fiber support is presented, which is well suited to the electrophoretic transfer of proteins from polyacrylamide gels and subsequent protein-chemical analysis. Modified glass-fiber sheets are easily prepared by chemical reaction of the surface with poly(methyl-3,3,3-trifluoropropylsiloxane) in trifluoroacetic acid. The modification is stable during electroblotting, amino acid sequence analysis and hydrolysis. The siliconized glass fiber exhibits a high protein-binding capacity, allows the application of well-established staining procedures, and does not interfere with the analytical methods of modern protein chemistry at the low picomole level. Samples separated by electrophoresis and immobilized on hydrophobic supports fail to exhibit any detectable contamination in amino acid sequence analysis hence allowing the high performance of the available protein-chemical methods to be exploited.
Eckerskorn
C
C
Max-Planck-Institut für Biochemie, Genzentrum, Martinsried, Federal Republic of Germany.
Mewes
W
W
Goretzki
H
H
Lottspeich
F
F
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D015153:Blotting, Western; D004129:Dimethylpolysiloxanes; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D005898:Glass; D007120:Immunochemistry; D008567:Membranes, Artificial; D011506:Proteins / Q000032:analysis*; D012828:Silicones; D013194:Staining and Labeling
D000596:Amino Acids; D004129:Dimethylpolysiloxanes; D008567:Membranes, Artificial; D011506:Proteins; D012828:Silicones; C009753:fiberglass; C049525:polymethyl-3,3,3-trifluoropropylsiloxane