Document Detail

The effect of the presence of the metal prosthetic groups on the subunit structure of bovine superoxide dismutase in sodium dodecyl sulfate.
MedLine Citation:
PMID:  1197385     Owner:  NLM     Status:  MEDLINE    
Dissociation into protomers of bovine superoxide dismutase by sodium dodecyl sulfate (SDS) depends on the metal prosthetic group and incubation time in the presence of detergent. The holoenzyme containing either copper and zinc or copper and cobalt is not dissociated. The fully metal-free apoenzyme is dissociated into protomers after short preincubation in SDS. The copper-free enzyme, still containing zinc or cobalt, is dissociated to a significant extent only after 24 hours preincubation in SDS. This effect is associated with a gradual alteration of the native zinc site, as followed by optical spectra of the homologous cobalt enzyme. Removal of SDS results in significant reassociation of protomers which is apparently independent of the presence of metals.
F Marmocchi; G Caulini; G Venardi; D Cocco; L Calabrese; G Rotilio
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Physiological chemistry and physics     Volume:  7     ISSN:  0031-9325     ISO Abbreviation:  Physiol. Chem. Phys.     Publication Date:  1975  
Date Detail:
Created Date:  1976-02-26     Completed Date:  1976-02-26     Revised Date:  2004-11-17    
Medline Journal Info:
Nlm Unique ID:  0202364     Medline TA:  Physiol Chem Phys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  465-71     Citation Subset:  IM    
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MeSH Terms
Binding Sites
Cobalt / analysis*
Copper / analysis*
Macromolecular Substances
Molecular Weight
Protein Binding
Sodium Dodecyl Sulfate*
Superoxide Dismutase* / analysis
Zinc / analysis*
Reg. No./Substance:
0/Macromolecular Substances; 151-21-3/Sodium Dodecyl Sulfate; 7440-48-4/Cobalt; 7440-50-8/Copper; 7440-66-6/Zinc; EC Dismutase

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

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