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- W2423468049 abstract "pH dependence of binding properties of mitomycin derivatives to bovine serum albumin and some transport behaviors of mitonmycin derivatives aqueous solution through cellophane tube, were investigated in order to clarify the relationship between the chemical structure of mitomycin derivatives and their binding sites. As previous paper, investigated mitomycin derivatives were demethoxymitomycin-A, 7-amino-N-methylisomitomycin-B, mitomycin-C, decarbamoylmitomycin-C, and 10-acetoxydecarbamoylmitomycin-C. 1) Mitomycin derivatives are more labilized in acidic condition than in alkaline, and are relatively stable in the pH region of 6.0 to 10.0. Among these compounds, mitomycin-C is the most stable in the above pH range. 2) Diffusion coefficients of mitomycin derivatives at 25° in 0.05 M aqueous phosphate and borate buffer range from 0.3×10 to 0.4×10-5(cm2/sea), and it is found that transport processes of mitomycin derivatives through a cellophane tube are rate-determined by diffusion processes. 3) The Scatchard plot showed that mitomycin derivatives bind to bovine serum albumin at homogenous binding sites with 9 saturated binding sites at pH 8.0 as well as at pH 7.0. Association constants at pH 8.0 decrease to 1/1.6 to 1/3.3 times compared with these at pH 7.0, and especially marked decrease in association constants was observed for decarbamoylmitomycin-C and 10-acetoxydecarbamoylmitomycin-C." @default.
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- W2423468049 date "1974-01-01" @default.
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- W2423468049 title "Binding of Mitomycin Derivatives to Serum Albumin. II. Permeability Behavior of Mitomycin through Cellophane Membrane and Interaction between Mitomycin and Bovin Serum Albumin" @default.
- W2423468049 doi "https://doi.org/10.1248/yakushi1947.94.3_371" @default.
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