PURIFICATION AND PROPERTIES OF HUMAN PLACENTAL DIPEPTIDYL PEPTIDASE IV
スポンサーリンク
概要
- 論文の詳細を見る
Dipeptidyl peptidase ？ (EC 3.4.14.5 ; Gly-Pro-ρ-nitroanilidase) was purified 1840-fold from human placenta and characterized. The enzyme was solubilized from membrane fractions with Triton X100 and subjected to zinc acetate fractionation, hydroxylapatite chromatography, Sephacryl S-300 chromatography and then affinity chromatographies with Lentil Lectin-Sepharose 4B and Gly-Pro-NH-(CH_2)_6-NH-Sepharose 4B. Dipeptidyl peptidase ？ was completely separated from leucine aminopeptidase by the final affinity chromatography. The apparent molecular weight of the enzyme was estimated to be 350,000 by gel filtration. The purified enzyme gave a single band with a weight of 124,000 with sodium dodecyl sulfate (SDS) gel-electrophoresis, suggesting that the enzyme consists of three subunits. The isoelectric point of the enzyme was 4.4. The purified enzyme was most active at pH 8.0 with Gly-Pro-ρ-nitroanilide as substrate and the Km value for this substrate was 2.27mM.
- 社団法人日本産科婦人科学会の論文
- 1985-05-01
著者
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Tomoda Yutaka
Department Of Biopharmaceutics Kyoto Pharmaceutical University
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Mizutani S
Department Of Obstetrics And Gynecology Nagoya University School Of Medicine
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Narita Osamu
Department Of Obstetrics And Gynecology Nagoya University School Of Medicine
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Mizutani Shigehiko
Department Of Obstetrics And Gynaecology Nagoya University School Of Medicine
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Tomoda Yutaka
Department Of Obstetrics And Gynecology And Research Institute Of Environmental Medicine Nagoya Univ
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Sumi Shigeharu
Department Of Obstetrics And Gynaecology Nagoya University School Of Medicine
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MIZYTANI Shigehiko
Department of Obstetrics and Gynaecology, Nagoya University School of Medicine
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Narita Osamu
Department Of Obstetrics And Gynaecology Nagoya University School Of Medicine
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