Enzymatic phosphorylation of soy globulins by the protein kinase CK2. Determination of the phosphorylation sites of beta-conglycinin alpha subunit by mass spectrometry.
Nahrung
; 42(3-4): 148-50, 1998 Aug.
Article
em En
| MEDLINE
| ID: mdl-9739557
ABSTRACT
Beta-conglycinin alpha subunit has been phosphorylated using a cAMP-independent protein kinase (CK2) purified from the yeast Yarrowia lipolytica. CK2 is known to phosphorylate serines and threonines in the consensus sequence Ser/Thr-X-X-Asp/Glu. Only 0.5 to 1 mol P/mol alpha subunit was incorporated although seven consensus sequences are present. Phosphorylated beta-conglycinin alpha subunit (P-alpha) was digested by trypsin. The resulting peptides were analysed by RP-HPLC coupled to electrospray ionisation mass spectrometry (LC-ESMS). Two phosphopeptides were identified corresponding to 70-89 and 116-127 sequences with Ser 75 and Ser 117 phosphorylated respectively. Ser 75 is one of the predicted phosphorylation sites according to the consensus sequence criteria. Ser 117 is inside a very acidic peptide but does not belong to a previously described consensus sequence.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Glycine max
/
Proteínas Serina-Treonina Quinases
/
Proteínas de Soja
/
Globulinas
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Nahrung
Ano de publicação:
1998
Tipo de documento:
Article
País de afiliação:
França