| Immunochemical studies on Rhodotorula gracilis D-amino acid oxidase. | |
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MedLine Citation:
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PMID: 1672654 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Polyclonal antibodies were prepared from rabbit sera after immunization with holo- and apo-D-amino acid oxidase purified from R. gracilis. Both anti-holo- and anti-apoenzyme IgG fractions (as well as affinity-purified IgG) were highly specific: in blot-transfer analyses after SDS-PAGE only a 39 kDa band, corresponding to enzyme monomer, was recognized even in the partially purified yeast extract. No cross-reaction was detected with pig kidney D-amino acid oxidase. As a difference from the mammalian enzyme, yeast D-amino acid oxidase anti-holo- and anti-apoenzyme IgGs had different properties in inactivation and precipitation experiments, indicating the existence of different antigenicity sites related to the FAD-binding domain in the enzyme. |
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Authors:
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L Pollegioni; M P Simonetta |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Experientia Volume: 47 ISSN: 0014-4754 ISO Abbreviation: Experientia Publication Date: 1991 Mar |
Date Detail:
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Created Date: 1991-05-03 Completed Date: 1991-05-03 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 0376547 Medline TA: Experientia Country: SWITZERLAND |
Other Details:
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Languages: eng Pagination: 232-5 Citation Subset: IM |
Affiliation:
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Department of General Physiology and Biochemistry, University of Milano, Italy. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Blotting, Western D-Amino-Acid Oxidase / metabolism* Electrophoresis, Polyacrylamide Gel Immunodiffusion Immunohistochemistry Precipitin Tests Rhodotorula / enzymology* Substrate Specificity |
| Chemical | |
Reg. No./Substance:
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EC 1.4.3.3/D-Amino-Acid Oxidase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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