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- W972541567 abstract "Publisher Summary This chapter presents data on the use of 1-Guanyl-3,5-dimethylpyrazole nitrate (GDMP) for guanidinating various proteins and, wherever possible, compares the results with those obtained with O-methylisourea (MIU). GDMP exists as colorless prisms, mp 166-168°. It is found GDMP to be susceptible to hydrolytic deguanylation with the formation of 3,5-dimethylpyrazole and urea. Slow destruction of the reagent followed a first-order reaction mechanism and is temperature-dependent. As in the guanidination of proteins with MIU, the reaction with GDMP depends on several factors, for example, pH, temperature, and concentration of reagent. The behavior of proteins toward GDMP reflects their unique structural features and may result in the development of physicochemical differences between native and guanidinated proteins. The rate of reaction of GDMP with the free amino groups of proteins increases rapidly with increase in pH, indicating that the reaction involves the uncharged form of one or both of the reactants. Owing to differences in behavior of proteins on guanidination with GDMP, representative conditions for three proteins are presented in the chapter." @default.
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- W972541567 date "1972-01-01" @default.
- W972541567 modified "2023-10-18" @default.
- W972541567 title "[51] Guanidination of proteins" @default.
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- W972541567 doi "https://doi.org/10.1016/s0076-6879(72)25055-8" @default.
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