[Studies on the activity and immunohistochemistry of heme oxygenase in Schistosoma japonicum].
OBJECTIVE
To explore the activity of heme oxygenase and immunolocate the enzyme in the adult worms of Schistosoma japonicum.


METHODS
Microsomal protein was isolated from the homogenate of adult S. japonicum, heme degradation and effect of different pH conditions and buffers on degrading reaction were investigated by incubating microsomal protein with hemin. The slices of whole worm and cells of S. japonicum were prepared, distribution of HO in schistosome was studied by immunofluorescent and alkaline phosphatase(AP)-immunocytochemical assays.


RESULTS
Microsomal protein of adult worms can degrade the heme in vitro, the activity being 56.7 nmol bilirubin/(mg.min). The optimal pH was 8.7. Immunofluorescent and AP-immunocytochemical assays revealed that the HO distributed dispersively in the worm, and located in cytoplasm.


CONCLUSIONS
The presence of HO was firstly proved in S. japonicum.
Liu
W Q
WQ
Department of Parasitology, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030.
Li
Y L
YL
Ruppel
A
A
D000818:Animals; D003593:Cytoplasm / Q000201:enzymology; D006418:Heme / Q000378:metabolism; D006419:Heme Oxygenase (Decyclizing) / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007150:Immunohistochemistry; D051379:Mice; D012549:Schistosoma japonicum / Q000201:enzymology*
D006418:Heme; D006419:Heme Oxygenase (Decyclizing)