Synthesis of Chromogenic Substrates Specific for Human Spleen Fibrinolytic Proteinase (SFP) and Human Leukocyte Elastase (LE)

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概要

• 論文の詳細を見る

• Various peptide anilides were synthesized by a conventional method with the object of obtaining specific substrates for human spleen fibrinolytic proteinase (SFP) and human leukocyte elastase (LE) in order to compare the substrate specificity of SFP with that of LE. It was found that the P_1 Val compound among succinyl tripeptide p-nitroanilides (Suc-Tyr-Leu-X-pNA) exhibited the highest k_<cat>/K_m values for hydrolysis by SFP and LE, however, the tetrapeptide Suc-Ala-Tyr-Leu-Val-pNA [k_<cat>/K_m values (M^<-1>S^<-1>) for hydrolysis by SFP and LE : 84000 and 48000,respectively] was the preferred chromogenic substrate for SFP and LE because of its high solubility in the buffer and its moderate k_<cat>/K_m values. The substrate specificity of SFP was found to be similar to that of LE.

• 社団法人日本薬学会の論文
• 1982-11-25

著者

• 岡田 芳男

  Faculty of Pharmaceutical Sciences Kobe-Gakuin University

• 津田 裕子

  Faculty of Pharmaceutical Sciences

• 永松 陽子

  Faculty Of Nutrition Kobe-gakuin University

• 岡本 歌子

  Faculty of Pharmaceutical Sciences

• 平田 昭夫

  Faculty of Pharmaceutical Sciences, Kobe-Gakuin University

• 平田 昭夫

  Faculty Of Pharmaceutical Sciences Kobe-gakuin University

• 津田 裕子

  神戸学院大学薬学部薬品化学

• 岡本 歌子

  血栓止血研究神戸プロジェクト

関連論文

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