TY - JOUR
T1 - Plasmodium falciparum
T2 - Discovery of peroxidase active organelles
AU - McIntosh, Michael T.
AU - Elliott, David A.
AU - Joiner, Keith A.
N1 - Funding Information:
The authors gratefully thank the members of K.A. Joiner lab for helpful discussions during the course of this work. We are grateful to Dr. Katja Becker at Giessen University in Germany, for sharing her insights and observations on peroxiredoxins and for gifts of recombinant PfTPx1 and PfTPx2. This work was supported by grants from the Ellison Foundation and the Burroughs Wellcome Fund New Initiatives in Malaria Research awarded to K.A.J.
PY - 2005/10
Y1 - 2005/10
N2 - Staining with 3,3′ diaminobenzidine tetrahydrochloride (DAB) is a common method used for the detection of peroxidases. Using this histochemical staining method in conjunction with transmission electron microscopy, we observed oxidation of DAB that was localized to a discrete set of organelles displaying morphological similarity to small (75-90 nm diameter) versions of higher eukaryotic microbodies or peroxisomes. These single membrane bounded organelles were characterized by an asymmetrical matrix capable of oxidizing DAB to an electron dense inclusion. Oxidation of DAB was further found to be dependent upon hydrogen peroxide (H2O2) as a substrate. Given a lack of peroxisomal import proteins and enzymes, it is unlikely that these represent conventional peroxisomes. Rather, they likely represent specialized organelles containing endogenous peroxidase or pseudo-peroxidase activity.
AB - Staining with 3,3′ diaminobenzidine tetrahydrochloride (DAB) is a common method used for the detection of peroxidases. Using this histochemical staining method in conjunction with transmission electron microscopy, we observed oxidation of DAB that was localized to a discrete set of organelles displaying morphological similarity to small (75-90 nm diameter) versions of higher eukaryotic microbodies or peroxisomes. These single membrane bounded organelles were characterized by an asymmetrical matrix capable of oxidizing DAB to an electron dense inclusion. Oxidation of DAB was further found to be dependent upon hydrogen peroxide (H2O2) as a substrate. Given a lack of peroxisomal import proteins and enzymes, it is unlikely that these represent conventional peroxisomes. Rather, they likely represent specialized organelles containing endogenous peroxidase or pseudo-peroxidase activity.
UR - http://www.scopus.com/inward/record.url?scp=24644470428&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=24644470428&partnerID=8YFLogxK
U2 - 10.1016/j.exppara.2005.06.001
DO - 10.1016/j.exppara.2005.06.001
M3 - Article
C2 - 16039653
AN - SCOPUS:24644470428
SN - 0014-4894
VL - 111
SP - 133
EP - 136
JO - Experimental parasitology
JF - Experimental parasitology
IS - 2
ER -