Electronic Resource
Oxford, UK
:
Blackwell Publishing Ltd
The @journal of eukaryotic microbiology
32 (1985), S. 0
ISSN:
1550-7408
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Sodium dodecyl sulfate (SDS) and 2-mercaptoethanol (2-ME) activated proteolytic enzymes present in extracts of Entamoeba histolytica and E. invadens; SDS (0.5%) and 2-ME (1.4 and 715 mM) doubled the enzymatic activity when assayed on a stained insoluble substrate. Urea (4 M) did not reduce this activity, suggesting that amebic proteases are stable in the above denaturant conditions. Specific reagents for sulfhydryl (-SH) groups completely inhibited proteolytic activity regardless of pH. Inhibition with alkylating agents, such as N-ethylmaleimide and iodoacetamide, was reversed with 715 mM 2-ME as was also observed with papain. We conclude from these results that the main proteolytic enzymes contained in extracts of E. histolytica and E. invadens are dependent on free thiol groups.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1550-7408.1985.tb03032.x
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