Document Detail


Comparative aspects of adenylic acid deaminase and aspartate-2-oxoglutarate aminotransferase.
MedLine Citation:
PMID:  318369     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. The content of adenylic acid deaminase and of aspartate-2-oxoglutarate aminotransferase of skeletal muscle tissue from a variety of animals has been determined. 2. White (fast) muscle contained large amounts of adenylic acid deaminase and red (slow) muscle contained large amounts of aspartate aminotransferase. There was a general inverse relationship between the adenylic acid deaminase and the aspartate aminotransferase content of muscles from various vertebrates. Thus, there is no simple correlation between the capacity to produce inosinic acid and ammonia from adenylic acid and the capacity to catalyse the formation of aspartate for conversion of inosinic acid back to adenylic acid. 3. The absence of adenylic acid deaminase from the tail muscles of the yabbie and other invertebrates indicates a marked difference in the Animal Kingdom.
Authors:
S I Chandrasena; F J Hird
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Comparative biochemistry and physiology. B, Comparative biochemistry     Volume:  61     ISSN:  0305-0491     ISO Abbreviation:  Comp. Biochem. Physiol., B     Publication Date:  1978  
Date Detail:
Created Date:  1989-07-27     Completed Date:  1989-07-27     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2984730R     Medline TA:  Comp Biochem Physiol B     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  191-4     Citation Subset:  IM    
Affiliation:
Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria, Australia.
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MeSH Terms
Descriptor/Qualifier:
AMP Deaminase / metabolism*
Animals
Aspartate Aminotransferases / metabolism*
Male
Muscles / enzymology*
Nucleotide Deaminases / metabolism*
Rats
Chemical
Reg. No./Substance:
EC 2.6.1.1/Aspartate Aminotransferases; EC 3.5.4.-/Nucleotide Deaminases; EC 3.5.4.6/AMP Deaminase

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


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