| A comparative polyacrylamide gel electrophoretic study of arginase in vertebrate tissues. | |
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MedLine Citation:
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PMID: 6851990 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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G Venkatakrishnan; S R Reddy |
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: Enzyme Volume: 29 ISSN: 0013-9432 ISO Abbreviation: Enzyme Publication Date: 1983 |
Date Detail:
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Created Date: 1983-07-15 Completed Date: 1983-07-15 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 1262265 Medline TA: Enzyme Country: SWITZERLAND |
Other Details:
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Languages: eng Pagination: 145-52 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Animals Arginase / analysis* Electrophoresis, Polyacrylamide Gel Isoenzymes / analysis* Species Specificity Tissue Distribution |
| Chemical | |
Reg. No./Substance:
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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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