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PHOSPHORYLATION OF BETA-LACTOGLOBULIN USING AMINO-ACIDS AS THE SOLE BASE AND NUCLEOPHILE OF THE REACTION
Faculty
Agriculture
Year:
1995
Type of Publication:
Article
Pages:
145-150
Authors:
SITOHY, M, CHOBERT, JM, HAERTLE, T
DOI:
10.1007/BF01980326
Journal:
JOURNAL OF PROTEIN CHEMISTRY PLENUM PUBL CORP
Volume:
14
Research Area:
Biochemistry \& Molecular Biology
ISSN
ISI:A1995RA93900005
Keywords :
PHOSPHORYLATION, BETA-LACTOGLOBULIN, AMINO ACIDS
Abstract:
beta-Lactoglobulin was phosphorylated with 20, 40, and 80 mol of POCl3/mol protein in the presence of 4, 5, and 6 molar excess of basic amino acid per mol POCl3. Maximal phosphorylation yields of 5 and 3 mol P/mol protein were achieved when the highest stoichiometries of POCl3/arginine and lysine were used. Proportional high amounts of basic amino acids were also grafted to the protein molecule during its phosphorylation through the phosphoamide bond. Modified proteins displayed increased negative charges and reduced isoelectric points and were monomeric. The phosphorylated and phosphoamidated beta-lactoglobulin showed improved functional properties.
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