Prolyl endopeptidase purified from granulomatous inflammation in mice
作者： Yukinori Nozaki , Naoyoshi Sato , Toshihiro Iida , Kenji Hara , Kimie Fukuyama
关键词: Renin–angiotensin system 、 Enzyme 、 Angiotensin-converting enzyme 、 Angiotensin II 、 Prolyl endopeptidase 、 Biology 、 Biochemistry 、 Immunohistochemistry 、 Inflammation 、 Antibody 、 Cell biology 、 Molecular biology
摘要: Activity of prolyl endopeptidase (EC 3.4.21.26) which hydrolyses the Pro7-Phe8 bond in angiotensin II has been found to elevate experimentally produced granulomatous inflammation liver and skin. We purified enzyme 1,536-fold by 6 steps from murine hepatic granulomas. The a molecular weight 79 kDa physiocochemical properties equivalent those previously reported for other sources. By HPLC analysis, cleavage Phe8-Leu10 Phe8 I II, respectively, was detected quantified. Monospecific IgG prepared serum rabbits injected with enzyme. Concentration immunohistochemically cells form organization, but not inflammatory surrounding foci. antibody, however, cross reacted adjacent weakly stained their cytoplasm. findings indicate that this enzyme, addition converting may serve as useful biochemical marker tissue reactions.
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