Document Detail


Trypsin adsorption by Hymenolepis diminuta (Cestoda).
MedLine Citation:
PMID:  6154136     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Significant amounts of radioactivity were associated with Hymenolepis diminuta following incubation in 3H-trypsin. Autoradiography of worms incubated in 3H-trypsin for 30 min demonstrated that all radioactivity was associated with the worm's surface (tegument). The amount of 3H-trypsin adsorbed by the worms was not sufficient to account for the inactivation of this enzyme in the presence of intact worms. Unlabeled trypsin and poly-L-glutamate (but not poly-L-lysine) inhibited adsorption of 3H-trypsin, but were without effect on trypsin inactivation by H. diminuta. Therefore, trypsin was adsorbed by intact H. diminuta, but the process of adsorption apparently did not play any role in inactivation of the enzyme.
Authors:
L L Schroeder; P W Pappas
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.    
Journal Detail:
Title:  The Journal of parasitology     Volume:  66     ISSN:  0022-3395     ISO Abbreviation:  J. Parasitol.     Publication Date:  1980 Feb 
Date Detail:
Created Date:  1980-06-25     Completed Date:  1980-06-25     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  7803124     Medline TA:  J Parasitol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  49-52     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adsorption
Animals
Hymenolepis / enzymology*
Polyglutamic Acid / pharmacology
Polylysine / pharmacology
Trypsin / metabolism*
Trypsin Inhibitors
Chemical
Reg. No./Substance:
0/Trypsin Inhibitors; 25104-18-1/Polylysine; 25513-46-6/Polyglutamic Acid; EC 3.4.21.4/Trypsin

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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