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Schistosoma mansoni cathepsin D1: biochemical and biophysical characterization of the recombinant enzyme expressed in HEK293T cells

Abstract:

Schistosomes express a variety of aspartyl proteases (APs) with distinct roles in the helminth pathophysiology, among which degradation of host haemoglobin is key, since it is the main amino acid source for these parasites. A cathepsin D-like AP from Schistosoma mansoni (SmCD1) has been used as a model enzyme for vaccine and drug development studies in schistosomes and yet a reliable expression system for readily producing the recombinant enzyme in high yield has not been reported. To contrib...

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Publication status:
Published
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.pep.2019.105532

Authors


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Role:
Author
ORCID:
0000-0002-4587-4620
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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Structural Biology
Role:
Author
ORCID:
0000-0002-3705-2993
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Name:
Medical Research Council
Grant:
MR/M026221/1
Publisher:
Elsevier
Journal:
Protein Expression and Purification More from this journal
Volume:
167
Article number:
105532
Publication date:
2019-11-08
Acceptance date:
2019-11-07
DOI:
EISSN:
1096-0279
ISSN:
1046-5928
Pmid:
31711796
Language:
English
Keywords:
Pubs id:
pubs:1074809
UUID:
uuid:8c748ef2-8a02-4e1b-829e-50e613bf4496
Local pid:
pubs:1074809
Source identifiers:
1074809
Deposit date:
2020-01-10

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