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Originally published In Press as doi:10.1074/jbc.M002809200 on June 7, 2000

J. Biol. Chem., Vol. 275, Issue 34, 26109-26112, August 25, 2000
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Specific Glutamine and Asparagine Residues of gamma -S Crystallin Are Resistant to in Vivo Deamidation*

Larry TakemotoDagger and Daniel Boyle

From the Division of Biology, Ackert Hall, Kansas State University, Manhattan, Kansas 66506

It has been hypothesized that resistance to nonenzymatic deamidation of asparagine and glutamine residues may be an important determinant of protein stability in vivo. As a test of this hypothesis, we analyzed the central region of old human lenses, which contain proteins such as gamma -S crystallin that were synthesized during the fetal-embryonic periods of development. Total protein from the fetal-embryonic region of old human lenses was digested with trypsin, followed by resolution of tryptic fragments containing amidated and deamidated forms using high pressure liquid chromatography-reverse phase chromatography together with synthetic peptide standards and mass spectral analysis. The results demonstrate no detectable deamidation of glutamine 92, glutamine 96, asparagine 143, and glutamine 170 from gamma -S crystallin from old human lenses, consistent with the hypothesis that very long-lived proteins can contain asparagine and glutamine residues that are extremely resistant to in vivo deamidation.

* This study was supported by Grant 2 RO1 EY02932-19 from the National Institutes of Health (to L. T.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Tel.: 785-532-6811; Fax: 785-532-6799; E-mail: takemlj@ksu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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