Document Detail


Immunochemical studies on Rhodotorula gracilis D-amino acid oxidase.
MedLine Citation:
PMID:  1672654     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
L Pollegioni; M P Simonetta
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Experientia     Volume:  47     ISSN:  0014-4754     ISO Abbreviation:  Experientia     Publication Date:  1991 Mar 
Date Detail:
Created Date:  1991-05-03     Completed Date:  1991-05-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0376547     Medline TA:  Experientia     Country:  SWITZERLAND    
Other Details:
Languages:  eng     Pagination:  232-5     Citation Subset:  IM    
Affiliation:
Department of General Physiology and Biochemistry, University of Milano, Italy.
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MeSH Terms
Descriptor/Qualifier:
Blotting, Western
D-Amino-Acid Oxidase / metabolism*
Electrophoresis, Polyacrylamide Gel
Immunodiffusion
Immunohistochemistry
Precipitin Tests
Rhodotorula / enzymology*
Substrate Specificity
Chemical
Reg. No./Substance:
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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