The formation, isolation and importance of isopeptides in heated proteins.
The separation and resolution of the isopeptides Nepsilon (gamma-L-glutamyl)-L-lysine and Nepsilon (beta-aspertyl)-L-lysine, formed in heated proteins, has been successfully achieved. The method demands a well characterised ion-exchange column and the use of pH 3.40 lithium citrate buffer (O.2N Li+). Due to variations in particle size and percentage crosslinkages in the ion-exchange resin a computer assisted buffer gradient system has been developed. This system affects resolution of both isopeptides in 7h. The use of leucyl-glycine as an internal standard facilitates quantitative estimation of the isopeptides. This separative method has been used to analyse a series of heated protein samples and to estimate the quantities of isopeptides formed. The ability of a protein to form isopeptides links is discussed as well as the implication of such links on the reactivity and digestibility of proteins.
The formation, isolation and importance of isopeptides in heated proteins. The separation and resolution of the isopeptides Nepsilon (gamma-L-glutamyl)-L-lysine and Nepsilon (beta-aspertyl)-L-lysine, formed in heated proteins, has been successfully achieved. The method demands a well characterised ion-exchange column and the use of pH 3.40 lithium citrate buffer (O.2N Li+). Due to variations in particle size and percentage crosslinkages in the ion-exchange resin a computer assisted buffer gradient system has been developed. This system affects resolution of both isopeptides in 7h. The use of leucyl-glycine as an internal standard facilitates quantitative estimation of the isopeptides. This separative method has been used to analyse a series of heated protein samples and to estimate the quantities of isopeptides formed. The ability of a protein to form isopeptides links is discussed as well as the implication of such links on the reactivity and digestibility of proteins.