Document Detail


Involvement of polyphosphorylserine blocks in the Fe(III) binding by phosvitin.
MedLine Citation:
PMID:  975400     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
It has been suggested that the binding of iron(III) by phosvitin involves the phosphoric radicals of phosphorylserine residues, many of which are arranged in rows of several consecutive phosphoamino acids. In this paper we present evident that, unlike free phosphorylserine which does not interact with Fe(III), polyphosphorylserine blocks--(Ser-P)n, with n greater than or equal to 4 -- bind Fe(III) like phosvitin, though less actively, to give complexes stable at very acidic pHs. The binding of iron does not cause any polymerization of the phosphopeptides, and the (Ser-P)n-Fe(III) complexes display an Fe/P ratio significantly lower than 0.5, found in Fe-saturated phosvitin. These findings indicate that polyphosphorylserine blocks play an important role in the binding of iron by phosvitin, and that in the intact protein their binding capacity is optimized by the conformation of the polypeptide chain.
Authors:
A Donella; L A Pinna; V Moret
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Chemico-biological interactions     Volume:  15     ISSN:  0009-2797     ISO Abbreviation:  Chem. Biol. Interact.     Publication Date:  1976 Oct 
Date Detail:
Created Date:  1977-01-03     Completed Date:  1977-01-03     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0227276     Medline TA:  Chem Biol Interact     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  165-71     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Binding Sites
Egg Proteins*
Iron*
Kinetics
Molecular Weight
Organophosphorus Compounds
Oxidation-Reduction
Phosvitin*
Serine*
Chemical
Reg. No./Substance:
0/Egg Proteins; 0/Organophosphorus Compounds; 56-45-1/Serine; 7439-89-6/Iron; 9008-96-2/Phosvitin

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


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