| Comparative aspects of adenylic acid deaminase and aspartate-2-oxoglutarate aminotransferase. | |
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MedLine Citation:
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PMID: 318369 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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S I Chandrasena; F J Hird |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Comparative biochemistry and physiology. B, Comparative biochemistry Volume: 61 ISSN: 0305-0491 ISO Abbreviation: Comp. Biochem. Physiol., B Publication Date: 1978 |
Date Detail:
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Created Date: 1989-07-27 Completed Date: 1989-07-27 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 2984730R Medline TA: Comp Biochem Physiol B Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 191-4 Citation Subset: IM |
Affiliation:
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Russell Grimwade School of Biochemistry, University of Melbourne, Parkville, Victoria, Australia. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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AMP Deaminase
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metabolism* Animals Aspartate Aminotransferases / metabolism* Male Muscles / enzymology* Nucleotide Deaminases / metabolism* Rats |
| Chemical | |
Reg. No./Substance:
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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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