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AMINO-ACID GRAFTING OF BETA-LACTOGLOBULIN MEDIATED BY PHOSPHORUS OXYCHLORIDE
Faculty
Agriculture
Year:
1995
Type of Publication:
Article
Pages:
269-272
Authors:
SITOHY, M, CHOBERT, JM, HAERTLE, T
DOI:
10.1016/0141-8130(95)98154-Q
Journal:
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES BUTTERWORTH-HEINEMANN LTD
Volume:
17
Research Area:
Biochemistry \& Molecular Biology
ISSN
ISI:A1995RZ59100005
Keywords :
PHOSPHORYLATION, AMINO ACID GRAFTING, BETA-LACTOGLOBULIN
Abstract:
beta-Lactoglobulin was phosphorylated with 80 mot of POCl3/mol protein in the presence of triethylamine and amino acids or their esters added at a total molar excess of 6 mol base/mol POCl3. The extent of phosphorylation was reduced when the amino acids replaced triethylamine as the base. Arginine and lysine were grafted to protein molecules in amounts proportional to the beta-lactoglobulin phosphorylation, while histidine grafting was very weak. The electrophoretic patterns of the modified proteins showed increased negative charges, reduced isoionic points and slight dimerization. The emulsifying properties of the modified proteins were improved.
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