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Image Search Results
Journal: The Journal of biological chemistry
Article Title: The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding consensus sequence.
doi: 10.1074/jbc.272.20.13419
Figure Lengend Snippet: FIG. 2. Affinity chromatography of total rat brain homogenate on dynamin I deletion constructs. A, schematic drawing of the human dynamin Iaa deletion constructs used for the affinity purification. PRD, proline-rich domain. B, protein staining (Coomassie) of the SDS-PAGE gels of total brain homogenate (TH) and of the material eluted from the affinity columns. Lane numbers correspond to the number of the constructs shown in A. Heavy bands represent fusion proteins used as the immunoabsorbents. An arrow points to the amphiphysin bands visible in lanes 3 and 4. C, Western blotting with anti-amphiphysin antibodies of a gel identical to the one shown in B. The two immunoreactive bands (lanes 3 and 4) correspond to the two bands indicated by an arrow in B.
Article Snippet: Protein was measured using the BCA and
Techniques: Affinity Chromatography, Construct, Affinity Purification, Staining, SDS Page, Western Blot