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Non-Enzymatic Incorporation of Phosphate into Soya Bean Proteins

✍ Scribed by Chardot, T; Meunier, J C


Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
391 KB
Volume
72
Category
Article
ISSN
0022-5142

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✦ Synopsis


Soya bean reserve proteins were phosphorylated with iron111 and ATP or PP. In the case of ATP, a transfer of the triphosphate moiety to the protein was observed. This phosphorylation was very sensitive to the oxidation state and polynucleation of iron, no incorporation being observed with ironII. Up to 0.2 mol PP and 1-15 mol of iron per mole of /I-conglycinin, and 0-25 mol PP and 1.06 mol of iron per mole glycinin were incorporated. The phosphorylated proteins were stable under the conditions of TCA precipitation and high ionic strength. The chemical link was not likely to be a phosphoester as deduced from the acidic stability study. Phosphate was certainly incorporated as a complex with iron into the proteins.


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## Abstract Protein farnesyltransferase (PFTase) catalyzes the attachment of a geranyl azide moiety to a peptide substrate, N‐dansyl–Gly–Cys–Val–Ile–Ala–OH. The resulting azide‐containing peptide was derivatized with a triphenylphosphine‐based reagent to generate an O‐alkyl imidate‐linked product,