Document Detail

Proteolysis of interleukin-2, interferon and immunoglobulin by venoms.
MedLine Citation:
PMID:  1724747     Owner:  NLM     Status:  MEDLINE    
Limited proteolysis by venoms was analysed by the cleaved peptide band(s) in SDS-polyacrylamide gel electrophoresis. The venom from Crotalus atrox degraded interferon, interleukin-2, IgG, IgM, and a crude form of acetyl cholinesterase but had no effect on IgA. Although the venom from Androctonus australis did not exert appreciable proteolysis on any of the immunoglobulins it had potent proteolytic activities against interferon and interleukin-2. The venom from Vespula maculifrons had only a minor proteolytic effect on interferon. The proteolysis by venoms was not effectively inhibited by alpha 1-antitrypsin or a2-macroglobulin. Moreover, no appreciable proteolytic activity was detected in the venoms from Bufo arenarum, Apis mellifera and Heloderma suspectrum.
W N Kuo; U Ganesan; A Robinson; J R Flanders; M E Fausti; M N Jean; M L Gurnee; J Kuo
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Cytobios     Volume:  67     ISSN:  0011-4529     ISO Abbreviation:  Cytobios     Publication Date:  1991  
Date Detail:
Created Date:  1992-04-21     Completed Date:  1992-04-21     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0207227     Medline TA:  Cytobios     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  145-51     Citation Subset:  IM    
Division of Science and Mathematics, Bethune-Cookman College, Daytona Beach, Florida 32115.
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MeSH Terms
Electrophoresis, Polyacrylamide Gel
Endopeptidases / metabolism*
Immunoglobulin G / metabolism*
Interferons / metabolism*
Interleukin-2 / metabolism*
Venoms / metabolism*
Grant Support
Reg. No./Substance:
0/Immunoglobulin G; 0/Interleukin-2; 0/Venoms; 9008-11-1/Interferons; EC 3.4.-/Endopeptidases

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

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