Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5-Reference-Cited by-同舟云学术

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Mildly acidic conditions eliminate deamidation artifact during proteolysis: digestion with endoprotease Glu-C at pH 4.5

Published:2016-01-09 Issue:4 Volume:48 Page:1059-1067
ISSN:0939-4451
Container-title:Amino Acids
language:en
Short-container-title:Amino Acids

Author:

Liu Shanshan,Moulton Kevin Ryan,Auclair Jared Robert,Zhou Zhaohui Sunny

Funder

National Institutes of Health

Publisher

Springer Science and Business Media LLC

Subject

Organic Chemistry,Clinical Biochemistry,Biochemistry

Link

http://link.springer.com/content/pdf/10.1007/s00726-015-2166-z.pdf

Reference59 articles.

1. Alfaro JF et al (2008) Chemo-enzymatic detection of protein isoaspartate using protein isoaspartate methyltransferase and hydrazine trapping. Anal Chem 80:3882–3889. doi: 10.1021/ac800251q

2. Biastoff S, Teuber M, Zhou ZS, Dräger B (2006) Colorimetric activity measurement of a recombinant putrescine N-methyltransferase from datura stramonium. Planta Med 72:1136–1141. doi: 10.1055/s-2006-947191

3. Böhme L, Bär JW, Hoffmann T, Manhart S, Ludwig H-H, Rosche F, Demuth H-U (2008) Isoaspartate residues dramatically influence substrate recognition and turnover by proteases. Biol Chem 389:1043–1053. doi: 10.1515/bc.2008.123

4. Capasso S, Kirby AJ, Salvadori S, Sica F, Zagari A (1995) Kinetics and mechanism of the reversible isomerization of aspartic acid residues in tetrapeptides. J Chem Soc Perkin Trans 2:437–442. doi: 10.1039/P29950000437

5. Chen Z-W, Bergman T, Östenson C-G, Efendic S, Mutt V, Jörnvall H (1997) Characterization of dopuin, a polypeptide with special residue distributions. Eur J Biochem 249:518–522. doi: 10.1111/j.1432-1033.1997.t01-2-00518.x

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