著者

小山 岩雄 山上 治夫 桑江 豊保 倉田 宗司

出版者

公益社団法人 日本薬学会

雑誌

藥學雜誌 (ISSN:00316903)

巻号頁・発行日

vol.102, no.8, pp.796-799, 1982

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The contents of 6-keto-prostaglandin F<SUB>1&alpha;</SUB> (6KF<SUB>1&alpha;</SUB>) and thromboxane B<SUB>2</SUB> (TXB<SUB>2</SUB>) in mouse peritoneal macrophages were determined by radioimmunoassay. When indomethacin at a final concentration of 0.1 mM was added at each stage in the preparation of macrophage samples, i.e. (I) before incubation of peritoneal exudate cells in glass dishes to prepare macrophage monolayers, (II) before harvest of macrophages from the glass surfaces, (III) before sonication of macrophage suspensions, and (IV) before centrifugation of sonicated macrophage solutions, large differences were detected in the contents of 6KF<SUB>1&alpha;</SUB> and TXB<SUB>2</SUB> at each stage. These results suggested that physical stimulation during the preparation of samples resulted in increases of 6KF<SUB>1&alpha;</SUB> and TXB<SUB>2</SUB> production by macrophages.

著者

平原 敬三 安藤 直子 松石 哲郎 鈴木 信夫 寺尾 俊彦 倉田 宗司

出版者

公益社団法人日本薬学会

雑誌

薬学雑誌 (ISSN:00316903)

巻号頁・発行日

vol.108, no.9, pp.p860-866, 1988-09

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The addition of sodium oleate to antithrombin III (ATIII) produced complexes of ATIII and oleic acid by varying the acid concentration. During immunoelectrophoresis, ATIII shifted to the anode in the presence of sodium oleate. The reactivity of ATIII with anti human ATIII serum lowered as the sodium oleate level increased. However the reactivity with antibody obtained by immunization of rabbits with the mixture of sodium oleate and ATIII, was not lost on the immunoelectrophoresis. In acrylamide gel electrophoresis, ATIII separated into 6 bands with an increase in sodium oleate. The binding ratio of ATIII to heparin-Sepharose decresed in the presence of sodium oleate. In acrylamide gel isoelectrofocusing, the subtypes of ATIII having pI 5 showed high affinity to oleic acid. These high affinity subtypes also showed high affinity to heparin and thrombin. In fibrinogen agarose electrophoresis, ATIII lost its antithrombin activity depending on the increase of sodium oleate. By the determination of free fatty acids (FFA) in ATIII purified from normal plasma, we found that FFA would bind to ATIII in the normal plasma. Scatchard plot analysis indicated 7.6 binding sites of oleic acid per ATIII molecule. The results suggested that ATIII lost its activity by conformational change or interference in the thrombin binding site, and that the subtype of ATIII having pI 5 could be a significant carrier of plasma FFA.