Document Detail

Heterogeneity of dipeptidyl peptidase IV from C6 rat glioma cells.
MedLine Citation:
PMID:  10985474     Owner:  NLM     Status:  MEDLINE    
Dipeptidyl peptidase IV is known to be involved, due to both hydrolytic and non-hydrolytic mechanisms, in various cell functions of normal and cancer cells as well. In this report dipeptidyl peptidase IV substrate and pH preferences, some inhibition parameters, freezing/thawing sensitivity and stability against hydrolysis by trypsin were studied in C6 rat glioma cells. Our results confirmed substantial heterogeneity of dipeptidyl peptidase IV population. Such observation is important to avoid methodological artifacts and to decrease risk of misinterpretations in biological studies.
R Malík; L Vlasicová; L Kadlecová; A Sedo
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Neoplasma     Volume:  47     ISSN:  0028-2685     ISO Abbreviation:  Neoplasma     Publication Date:  2000  
Date Detail:
Created Date:  2000-09-15     Completed Date:  2000-09-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0377266     Medline TA:  Neoplasma     Country:  SLOVAKIA    
Other Details:
Languages:  eng     Pagination:  96-9     Citation Subset:  IM    
1st Department of Medical Chemistry and Biochemistry, 1st Faculty of Medicine, Charles University, Prague 2, Czech Republic.
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MeSH Terms
Antigens, CD26 / metabolism*
Enzyme Stability
Glioma / enzymology*
Hydrogen-Ion Concentration
Isoleucine / analogs & derivatives*,  pharmacology
Oligopeptides / pharmacology
Protease Inhibitors / pharmacology
Substrate Specificity
Thiazoles / pharmacology
Trypsin / metabolism,  pharmacology
Tumor Cells, Cultured
Reg. No./Substance:
0/Oligopeptides; 0/Protease Inhibitors; 0/Thiazoles; 0/isoleucyl-thiazolidide; 73-32-5/Isoleucine; 90614-48-5/diprotin A; 90614-49-6/diprotin B; EC, CD26; EC

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