Home > Research > Publications & Outputs > Characterization of developmentally-regulated n...
View graph of relations

Characterization of developmentally-regulated nucleases in promastigotes and amastigotes of Leishmania mexicana

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Published

Standard

Characterization of developmentally-regulated nucleases in promastigotes and amastigotes of Leishmania mexicana. / Bates, P A.
In: FEMS Microbiology Letters, Vol. 107, No. 1, 02.1993, p. 53-58.

Research output: Contribution to Journal/MagazineJournal articlepeer-review

Harvard

APA

Vancouver

Bates PA. Characterization of developmentally-regulated nucleases in promastigotes and amastigotes of Leishmania mexicana. FEMS Microbiology Letters. 1993 Feb;107(1):53-58. doi: 10.1111/j.1574-6968.1993.tb06003.x

Author

Bibtex

@article{2c3c91f2551b467e82bb987414b6d4c1,
title = "Characterization of developmentally-regulated nucleases in promastigotes and amastigotes of Leishmania mexicana",
abstract = "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.",
keywords = "Leishmania mexicana, Nucleotidase , Nuclease",
author = "Bates, {P A}",
year = "1993",
month = feb,
doi = "10.1111/j.1574-6968.1993.tb06003.x",
language = "English",
volume = "107",
pages = "53--58",
journal = "FEMS Microbiology Letters",
issn = "0378-1097",
publisher = "Wiley-Blackwell",
number = "1",

}

RIS

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 -