"Low-Molecular Kininogen"類似ペプチドのモルモット回腸収縮作用とTrypsinとの関係

概要

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The action of three synthesized peptides allied to bradykinin, i.e., [Ser(Ac)^6]-bradykinyl-Gly-Val-Gln (III), Gly-Gly-Lys-[Ser(Ac)^6]-bradykinin (IV), and bradykinylglycine (V), for contraction of excised ileum of a guinea pig was compared with that of bradykinin (I). Activities of these peptides after incubation with trypsin (pH 8.0) at 37° for 50 min was examined with ileum contracting action as the indicator in order to examine their properties as the so-called "low-molecular kininogen" -like peptides. IV possessed a comparatively strong activity, being 3.5% of that of I but that of III and V was weak, being 0.03% and 0.14% of I. Trypsin treatment markedly increased the activity, that of III becoming 67% and that of IV to 32% of I. This fact suggests that trypsin treatment has effected not only the liberation of [Ser(Ac)^6]-bradykinin (II) but hydrolysis of the ester in the O-acetylserine residue also occurred at the same time to liberate I. The activity of V after its trypsin treatment was 2.3% of that of I. Comparison of this fact with the trypsin treatment of III suggests that when a free carboxyl group is present in the glycine residue of C-terminal arginine-glycine bond in V, it seems difficult for trypsin to sever the peptide chain.
公益社団法人日本薬学会の論文
1971-01-25