Effects of Drug Binding on the Esterase-like Activity of Human Serum Albumin. VI. Reaction with Di-p-nitrophenyl Adipate
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概要
- 論文の詳細を見る
The binding of R type drugs, which have high affinity to a site (R site) near the tyrosine-411 residue, remarkably accelerated the reaction of di-p-nitrophenyl adipate (D) with human serum albumin (HSA). The reaction was investigated kinetically at various pHs and 25℃. The reaction in the presence of an excess of HSA over D proceeded in two steps. The pH-profiles for both rate constants were sigmoidal, indicating the participation of two tyrosine residues having pK_a values of about 9.3 in the reactions. The two residues of HSA involved seem to be separated by a distance corresponding to the length of the adipoyl group.
- 公益社団法人日本薬学会の論文
- 1985-09-25
著者
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黒野 幸久
神戸大学 大学院医学系研究科精神神経科学分野
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池田 憲
名古屋市立大学薬学部
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池田 憲
Faculty Of Pharmaceutical Sciences Nagoya City University
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黒野 幸久
Faculty of Pharmaceutical Sciences, Nagoya City University
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杉浦 仁美
Faculty Of Pharmaceutical Sciences Nagoya City University
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