Molecular signatures of long-lived proteins: autolytic cleavage adjacent to serine residues
Article first published online: 23 AUG 2012
© 2012 The Authors. Aging Cell © 2012 Blackwell Publishing Ltd/Anatomical Society of Great Britain and Ireland
Volume 11, Issue 6, pages 1125–1127, December 2012
How to Cite
Su, S.-P., Lyons, B., Friedrich, M., McArthur, J. D., Song, X., Xavier, D., Truscott, R. J. W. and Aquilina, J. A. (2012), Molecular signatures of long-lived proteins: autolytic cleavage adjacent to serine residues. Aging Cell, 11: 1125–1127. doi: 10.1111/j.1474-9726.2012.00860.x
- Issue published online: 15 NOV 2012
- Article first published online: 23 AUG 2012
- Accepted manuscript online: 17 JUL 2012 11:43AM EST
- Accepted for publication 6 July 2012
Fig. S1 Endogenous low molecular weight peptides identified in the lens derived from cleavage of, (A) αA-crystallin, and (B) αB-crystallin.
Fig. S2 Endogenous low molecular weight peptides in the lens derived from cleavage of (A) βA1/A3-crystallin, (B) γS-crystallin, (C) βB1-crystallin and (D) βB2-crystallin.
Fig. S3 Protease activity is not detectable in the centre of older lenses.
Table S1 Endogenous LMW peptides present in human lens extracts.
Table S2 Totals of each of the 20 amino acid residues are tabulated as they occur in the combined sequences of all human lens crystallins – ƒP(protein).
Appendix S1 Experimental procedures.
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