Abstract:
: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.
journal_name
Chem Biol Interactjournal_title
Chemico-biological interactionsauthors
Donella A,Pinna LA,Moret Vdoi
10.1016/0009-2797(76)90161-7subject
Has Abstractpub_date
1976-10-02 00:00:00pages
165-71issue
2eissn
0009-2797issn
1872-7786pii
0009-2797(76)90161-7journal_volume
15pub_type
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journal_title:Chemico-biological interactions
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journal_title:Chemico-biological interactions
pub_type: 杂志文章,评审
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