Abstract
Publisher Summary N ɛ -(β-aspartyl)lysine cross-linking is generally found only in heated proteins. N ɛ -(β-Aspartyl)lysine has also been found in the urine of children with various pathological conditions, but its presence does not appear to be related to specific symptoms. The occurrence of β-Asp-ɛ-Lys links in native wool is doubtful. It is known that proteins from blood serum membranes, may accumulate in colostrum, and it is natural to predict that the products of the reactions catalyzed by these enzymes might also be detected in colostrum. When colostrums was screened for the presence of isopeptide bonds, not only the γ-Glu- ɛ-Lys link, but also the β-Asp-ɛ-Lys link, could be detected, however, only in a limited number of samples. The methods used to detect isopeptides include complete enzymatic digestion of proteins, requiring long-time treatments at pH 2.0 and 8.2. Under these conditions, the rather labile β-Asp-amide bond may well be hydrolyzed to a certain extent and it is, thus, likely that small amounts of this derivative are overlooked.
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