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72449174514
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note
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Fr. II strongly hydrolyzed Pro-Phe-Arg-MCA, a substrate of tissue kallikrein, and this peptidase activity was markedly suppressed by treatment with 10 μM aprotinin. These results suggested that the platypus venom had trypsin- or kallikrein-type proteolytic activity.
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20
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72449197242
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For details, see Figures S1 and S16 in the Supporting Information
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For details, see Figures S1 and S16 in the Supporting Information.
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22
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72449174046
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note
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The concentrations of peptides 1 and 4 in the venom fluid were 230 and 46 μM, respectively, as estimated by RP-HPLC analyses.
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72449171248
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note
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50 45 μM). Meanwhile, none of the peptides showed rat mast cell degranulation (1 mg/mL) or hemolytic activity against rabbit and sheep red blood cells (0.4 mg/mL).
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