1-Cyclohexyl-5-n-Butyl-2,4,6-trioxoperhydropyrimidineのタンパク結合

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The binding of 1-cyclohexyl-5-n-butyl-2,4,6-trioxoperhydropyrimidine (BCP) to bovine serum albumin was investigated using equlibrium dialysis method. BCP appears to be bound to two groups of sites on albumin (n_1=1.02,n_2=6.98) with the values for K_1 of 108×10^3 M^<-1> and K_2 of 1.35×10^3 M^<-1>. It was demonstrated by the use of control human serum and crystallized human serum albumin that albumin had the most significant binding properties among the protein in human serum. The extent of binding was influenced by buffer constitution ; no significant difference in the binding with phosphate buffer, inhibitory effect with formate buffer, and with ammonium buffer, Cl^- ion was inhibitory and NH_4^+ ion was accelerating. With increasing pH values, a progressive decrease in their binding occurred between pH 4 and 10 where there was a marked decrease in the binding. By investigating the effect of phenylbutazone on BCP binding, it was observed that BCP had some common binding sites with phenylbutazone and the binding affinity of BCP on this sites was 4 times weaker than phenylbutazone.
公益社団法人日本薬学会の論文
1966-09-25