Research output: Contribution to Journal/Magazine › Journal article › peer-review
Research output: Contribution to Journal/Magazine › Journal article › peer-review
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TY - JOUR
T1 - Characterization of developmentally-regulated nucleases in promastigotes and amastigotes of Leishmania mexicana
AU - Bates, P A
PY - 1993/2
Y1 - 1993/2
N2 - The parasitic protozoon Leishmania mexicana was examined for the presence of 3'-nucleotidase/nuclease using substrate SDS-PAGE. Two activities were detected: one with an apparent molecular mass of 40 kDa, and a doublet of 29/31 kDa. The two enzymes showed differences in their levels of expression in the two life-cycle stages of parasite examined: the 29/31 kDa doublet was detected at 60-fold higher levels in the pathogenic amastigote stage, but was also expressed by promastigotes, whereas the 40 kDa activity was only detected in promastigotes. Both were capable of hydrolysing a variety of substrates including 3'-AMP and poly(A). However, the 29/31 kDa form showed a broader, unique substrate specificity in that it was also capable of digesting double-stranded RNA and DNA.
AB - The parasitic protozoon Leishmania mexicana was examined for the presence of 3'-nucleotidase/nuclease using substrate SDS-PAGE. Two activities were detected: one with an apparent molecular mass of 40 kDa, and a doublet of 29/31 kDa. The two enzymes showed differences in their levels of expression in the two life-cycle stages of parasite examined: the 29/31 kDa doublet was detected at 60-fold higher levels in the pathogenic amastigote stage, but was also expressed by promastigotes, whereas the 40 kDa activity was only detected in promastigotes. Both were capable of hydrolysing a variety of substrates including 3'-AMP and poly(A). However, the 29/31 kDa form showed a broader, unique substrate specificity in that it was also capable of digesting double-stranded RNA and DNA.
KW - Leishmania mexicana
KW - Nucleotidase
KW - Nuclease
U2 - 10.1111/j.1574-6968.1993.tb06003.x
DO - 10.1111/j.1574-6968.1993.tb06003.x
M3 - Journal article
C2 - 8385643
VL - 107
SP - 53
EP - 58
JO - FEMS Microbiology Letters
JF - FEMS Microbiology Letters
SN - 0378-1097
IS - 1
ER -