Evidence for a novel racemization process of an asparaginyl residue in mouse lysozyme under physiological conditions |
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| Authors: | K Ueno T Ueda K Sakai Y Abe N Hamasaki M Okamoto T Imoto |
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| Institution: | (1) Graduate School of Bioresource and Bioenvironmental Sciences, Kyushu University, Fukuoka 812-8581, Japan;(2) Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582, Japan;(3) Department of Clinical Chemistry and Laboratory Medicine, Graduate School of Medical Sciences, Kyushu University, Fukuoka 812-8582, Japan;(4) Department of Applied Microbial Technology, Faculty of Engineering, Sojo University, Kumamoto 860-0082, Japan |
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| Abstract: | We examined chemical reactions in mouse lysozyme after incubation under physiological conditions (pH 7 and 37°C). After incubation for 8 weeks, racemization was observed specifically at Asn127 among the 19 Asp/Asn residues in mouse lysozyme. Furthermore, analysis of the primary structure showed that the racemized residue was not Asp, but Asn, which demonstrates that deamidation and isomerization did not occur. These results mean that this racemization occurs without forming a succinimide intermediate. This is the first example of D-asparaginyl formation in a protein occurring during the racemization process under physiological conditions.Received 16 September 2004; received after revision 26 October 2004; accepted 12 November 2004 |
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| Keywords: | Deterioration mouse lysozyme protein aging racemization |
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