Some properties of Dirofilariaimmitis acid proteinase as compared with those of mammalian cathepsin D and pepsin

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概要

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• Some properties of Dirofilaria immitis acid proteinase were compared with mammalian cathepsin D and pepsin. The optimum pH of D. immitis acid proteinase was in the range of pH 2.8 to 3.4, whereas mammalian cathepsin D and porcine pepsin were 3.0 - 4.6 and around 2.0, respectively. When incubating in neutral pH at 50℃ for 10min, the activity of D. immitis proteinase was reduced to about 75% of the initial level, although that of cathepsin D did not change and that of pepsin was completely destroyed. D. immitis proteinase and cathepsin D hydrolyzed well human hemoglobin and myoglobin, whereas pepsin hydrolyzed human hemoglobin, bovine hemoglobin and cytochrome C. Pepstatin, a potent inhibitor of mammalian cathepsin D completely inhibited these three enzymes. However, the effect of pepstatin was abolished strongest on pepsin (5 × 10^<-8>). About 90% of the activity of pepsin was inactivated by diazoacetyl-DL-norleucine methyl ester (DAN) for 10min after beginning the reaction. Under the same condition, D. immitis proteinase was inactivated gradually, about 50% of the initial activity was inactivated 60min after the beginning of the experiment. However, cathepsin D was never affected by DAN even for after a 60min incubation. About 30% of the activity of pepsin was inactivated by first incubating the enzyme with 1.2-epoxy-3-(P-nitrophenoxy)-propane at 37℃ for 10 min, although D. immitis proteinase and cathepsin D were not affected. In conclusion, we confirmed that the D. immitis proteinase belongs to the aspartic proteinase group and is an intermediate type between cathepsin D and pepsin.

• 群馬大学の論文
• 1995-03-31

著者

• Sato Kumiko

  College Of Medical Care And Technology Gunma University

• KARA Fumiko

  College of Medical Care and Technology, Gunma University

• Kara Fumiko

  College Of Medical Care And Technology Gunma University

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• Some properties of Dirofilariaimmitis acid proteinase as compared with those of mammalian cathepsin D and pepsin

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