Document Detail


Location of intrinsic and inducible phenoloxidase activity in molluscan hemocyanin.
MedLine Citation:
PMID:  16904637     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The phenoloxidase (PO) activity of the hemocyanins (Hcs) from two molluscan species, the gastropod Helix pomatia (Hp) and the cephalopod Sepia officinalis (So), was studied. With catechol as substrate the Hcs showed a weak o-diPO activity, which was moderately enhanced on limited proteolysis with subtilisin. The sites in the Hc molecules mainly responsible for this activity were identified. The highest intrinsic o-diPO activity and also by far the highest level of induction were found in the functional units (FUs) Hp f and So g, isolated from Hp beta-Hc and So Hc (subunit 2), respectively. The results thus support the earlier conclusion, made on the basis of sequence homology between molluscan Hcs, that Hp f and So g are functional and structural analogues. The subtilisin treatment of Hp f also induced monoPO activity, considered to be at the origin of browning of the sample.
Authors:
Nurul Islam Siddiqui; Roland Forben Akosung; Constant Gielens
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-08-04
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  348     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-08-22     Completed Date:  2006-10-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1138-44     Citation Subset:  IM    
Affiliation:
Laboratory of Biochemistry, Chemistry Department, Katholieke Universiteit Leuven, Celestijnenlaan 200 G, 3001 Leuven-Heverlee, Belgium.
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MeSH Terms
Descriptor/Qualifier:
Animals
Catalysis
Enzyme Activation
Enzyme Induction
Helix (Snails) / enzymology*
Hemocyanin / chemistry*,  metabolism
Monophenol Monooxygenase / biosynthesis*,  metabolism
Oxidation-Reduction
Protein Structure, Tertiary
Sepia / enzymology*
Chemical
Reg. No./Substance:
9013-72-3/Hemocyanin; EC 1.14.18.1/Monophenol Monooxygenase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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