Document Detail


Purification and properties of alpha-D-mannosidase from the limpet, Patella vulgata.
MedLine Citation:
PMID:  4986964     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. alpha-Mannosidase from the limpet, Patella vulgata, was purified nearly 150-fold, with 40% recovery. beta-N-Acetylglucosaminidase was removed from the preparation by treatment with ethanol. The final product was virtually free from beta-galactosidase. 2. Limpet alpha-mannosidase was assayed at pH3.5 and at this pH it was necessary to add Zn(2+) for full activity. At pH5, the enzyme had the same activity in the presence or absence of added Zn(2+). 3. On incubation at acid pH, the enzyme underwent reversible inactivation, which was prevented by adding Zn(2+). 4. EDTA accelerated inactivation and the addition of Zn(2+) at once restored activity. No other cation was found to reactivate the enzyme. 5. Cl(-) had an unspecific effect on hydrolysis by limpet alpha-mannosidase. It increased the rate of reaction with substrate. The anion did not prevent or reverse inactivation by EDTA. 6. It is concluded that alpha-mannosidase is a metalloenzyme or enzyme-metal ion complex, dissociable at the pH of activity, and that it requires Zn(2+) specifically.
Authors:
S M Snaith; G A Levvy; A J Hay
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  The Biochemical journal     Volume:  117     ISSN:  0264-6021     ISO Abbreviation:  Biochem. J.     Publication Date:  1970 Mar 
Date Detail:
Created Date:  1970-08-04     Completed Date:  1970-08-04     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  2984726R     Medline TA:  Biochem J     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  129-37     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Chlorides
Edetic Acid
Enzyme Activation
Glycoside Hydrolases / analysis,  isolation & purification*
Hydrogen-Ion Concentration
Mollusca
Zinc
Chemical
Reg. No./Substance:
0/Chlorides; 60-00-4/Edetic Acid; 7440-66-6/Zinc; EC 3.2.1.-/Glycoside Hydrolases
Comments/Corrections

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