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Science 11 January 1974:
Vol. 183. no. 4120, p. 85
DOI: 10.1126/science.183.4120.85
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Articles

Primary Sequence Dependence of the Deamidation of Rabbit Muscle Aldolase

James H. McKerrow 1 and Arthur B. Robinson 1

1 Bonner Laboratory of Biology and Chemistry, University of California, San Diego, La Jolla 92037

The first-order deamidation half-time of the peptide, Gly-Ser-Asn-His-Gly in phosphate butler, pH 7.4, ionic strength at 0.2, 37.0°C, is 6.4 ± 0.5 days. This compares favorably with the in vivo deamidation half-time of 8 days for this sequence in rabbit muscle aldolase. This fact is discussed with respect to the general hypothesis that sequence-controlled deamidation of glutaminyl and asparaginylresidues is a mechanism by which molecular and organismic development and aging are timed.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Chronoregulation by Asparagine Deamidation.
S. J. Weintraub and B. E. Deverman (2007)
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Protein deamidation.
N. E. Robinson (2002)
PNAS 99, 5283-5288
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Prediction of protein deamidation rates from primary and three-dimensional structure.
N. E. Robinson and A. B. Robinson (2001)
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Molecular clocks.
N. E. Robinson and A. B. Robinson (2001)
PNAS 98, 944-949
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Deamidation of human proteins.
N. E. Robinson and A. B. Robinson (2001)
PNAS 98, 12409-12413
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Science. ISSN 0036-8075 (print), 1095-9203 (online)