Document Detail

The phenoloxidases of the ascomycete Podospora anserina. Structural differences between laccases of high and low molecular weight.
MedLine Citation:
PMID:  101375     Owner:  NLM     Status:  MEDLINE    
In order to investigate the extent of the relationship between the three copper-containing glycoproteins, laccases I, II and III (Mr70000, 80000 and 390000 respectively) of Podospora anserina, the following experiments were carried out on laccases II and III: (a) determination of amino acid composition; (b) determination of N-terminal and C-terminal amino acid; (c) determination of sugar composition; (d) dissociation studies on native and denatured laccases and also after removal of copper from the enzymes; (e) digestion of the carbohydrate moieties with the aid of glycosylhydrolases. A comparison between the results of these experiments and data previously obtained with laccase I allows the following conclusions to be drawn. 1. Laccases II and III are not identical. 2. Neither of these low molecular weight laccases are as complete molecules subunits of the oligomeric laccase I. 3. The possibility of partial identity of amino acid sequences of laccases I and III can not be excluded. 4. Laccase II possibly consists of subunits of Mr37000 whereas laccase III does not. 5. Digestion of 50% of the carbohydrate content leads to complete loss of serological specificity (serological reaction and cross reaction). This finding is discussed with regard to the possible role of the carbohydrate moiety as antigenic determinants and thus as the reason for the immunological relationship. As a consequence, at least three independent structural genes for laccases must be assumed.
W Minuth; M Klischies; K Esser
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  90     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  1978 Sep 
Date Detail:
Created Date:  1979-01-24     Completed Date:  1979-01-24     Revised Date:  2007-07-23    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  73-82     Citation Subset:  IM    
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MeSH Terms
Amino Acids / analysis
Ascomycota / enzymology*
Carbohydrates / analysis
Catechol Oxidase*
Molecular Weight
Peptide Fragments / analysis
Reg. No./Substance:
0/Amino Acids; 0/Carbohydrates; 0/Isoenzymes; 0/Peptide Fragments; EC Oxidase

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