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- W2107310463 abstract "GTP is known to be a potent inhibitor of the protein crosslinking activity of transglutaminase (TG), probably the most abundant G protein in the human red cell. Nucleotide binding to TG was examined by fluorescence spectroscopy and anisotropy in mixtures of TG with methylanthraniloyl analogs of GTP and GDP. A characteristic feature was the appearance of a major energy transfer band (λ exc, max = 290 nm, λ em = 444 nm) from protein tryptophans to the bound nucleotides. Quenching of the bound fluorophore (λ exc = 360 nm, λ em = 444 nm) by acrylamide was barely different from that of free ligand. However, major changes were observed in anisotropy, which was used to demonstrate a facile exchange between bound and free nucleotides and to evaluate affinity constants for the binding of methylanthraniloyl GTP and GDP to TG." @default.
- W2107310463 created "2016-06-24" @default.
- W2107310463 creator A5023311552 @default.
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- W2107310463 date "2000-06-27" @default.
- W2107310463 modified "2023-10-17" @default.
- W2107310463 title "Nucleotide binding by the erythrocyte transglutaminase/G <sub>h</sub> protein, probed with fluorescent analogs of GTP and GDP" @default.
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- W2107310463 doi "https://doi.org/10.1073/pnas.140210197" @default.
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