Document Detail


A comparative polyacrylamide gel electrophoretic study of arginase in vertebrate tissues.
MedLine Citation:
PMID:  6851990     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The electrophoretic behaviour of arginase in the tissue extracts of rat, beef, lizard and frog was studied by bidirectional polyacrylamide gel electrophoresis. The enzyme from rat liver and submaxillary gland migrated to the cathode with the activity concentrated in a single peak. Arginase from beef liver emerged as a single peak of anodal migration with a significant shoulder in the sample gel. Frog liver and kidney enzymes also appeared as single peaks with a distinct anodal movement. The activity in mammalian kidney and lizard liver and kidney resolved into two peaks of anodal migration suggesting the presence of two isoenzymes of arginase in these tissues.
Authors:
G Venkatakrishnan; S R Reddy
Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Enzyme     Volume:  29     ISSN:  0013-9432     ISO Abbreviation:  Enzyme     Publication Date:  1983  
Date Detail:
Created Date:  1983-07-15     Completed Date:  1983-07-15     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  1262265     Medline TA:  Enzyme     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  145-52     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Arginase / analysis*
Electrophoresis, Polyacrylamide Gel
Isoenzymes / analysis*
Species Specificity
Tissue Distribution
Chemical
Reg. No./Substance:
0/Isoenzymes; EC 3.5.3.1/Arginase

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


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