Document Detail


Horse alpha 2-macroglobulin. Circular dichroism studies of conformational changes upon reaction with proteinases and methylamine.
MedLine Citation:
PMID:  2441724     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The interaction of horse alpha 2-macroglobulin with methylamine, trypsin and cathepsin D was studied by circular dichroism in the far and near UV region, by polyacrylamide gel electrophoresis and by determination of its inhibitory activity. The CD spectra of horse alpha 2-macroglobulin resemble those of bovine und human alpha 2-macroglobulin. The CD spectra were changed in a different manner after the interaction of alpha 2-macroglobulin with methylamine, trypsin and inactive or active cathepsin D, indicating that more than one conformational change occurs. Cathepsin D activity was not affected by complex formation with horse alpha 2-macroglobulin. In contrast to the action of trypsin, treatment with methylamine did not increase the electrophoretic mobility of alpha 2-macroglobulin.
Authors:
T Lah; M Vihar; A Dubin; V Turk
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biological chemistry Hoppe-Seyler     Volume:  368     ISSN:  0177-3593     ISO Abbreviation:  Biol. Chem. Hoppe-Seyler     Publication Date:  1987 May 
Date Detail:
Created Date:  1987-10-22     Completed Date:  1987-10-22     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  8503054     Medline TA:  Biol Chem Hoppe Seyler     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  487-92     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Cathepsin D / metabolism
Circular Dichroism
Electrophoresis, Polyacrylamide Gel
Horses
Indicators and Reagents
Protein Binding
Protein Conformation
Spectrophotometry, Ultraviolet
Trypsin / metabolism
Trypsin Inhibitors / pharmacology
alpha-Macroglobulins / analysis*
Chemical
Reg. No./Substance:
0/Indicators and Reagents; 0/Trypsin Inhibitors; 0/alpha-Macroglobulins; EC 3.4.21.4/Trypsin; EC 3.4.23.5/Cathepsin D

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


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