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1 areful extraction of the XNA strand from the gel slice.
2 rried out on the protein recovered from each gel slice.
3 cised, and quantitatively extracted from the gel slices.
4 f phosphotyrosine were found in only 2 of 60 gel slices.
5 is, and tryptic peptides were extracted from gel slices and analyzed by liquid chromatography-tandem
7 t or heavy isotope-labeled reagents, and the gel slices are then combined and digested with proteases
8 peptides in a series of experiments using a gel slice containing only 200 ng (3 pmol) of human doubl
10 ed for Western blotting of cell lysates, and gel slices corresponding to reactive bands were subjecte
11 d electroelution of protein factors from the gel slices corresponding to the ribonucleoprotein comple
13 ethod involves homogenization of the excised gel slice (in Tris-EDTA buffer), containing the DNA frag
14 ations where the amount of DNA in an excised gel slice is limited or when contaminating differential
16 plexes and RNase ONE footprinting in situ in gel slices or by RNase H cleavage of complexes in soluti
17 proteins in solution, as well as proteins in gel slices, prior to proteolytic digestion and mass spec
18 el electrophoresis and subsequent elution of gel slices revealed the presence of three active moietie
21 tive DNA coupled with PCR amplification from gel slices, we show that specific binding sites can be i