Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation.

Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Research Abstract Details 

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Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Abstract Text:

Jason J Cournoyer,Cheng Lin,Michael J Bowman,Peter B O'Connor,

Relative quantitation of aspartyl and isoaspartyl residue mixtures from asparagine deamidation is demonstrated using electron capture dissociation without prior HPLC separation. The method utilizes the linear relationship found between the relative abundance of the isoaspartyl diagnostic ion, z(n)-57, and % isoaspartyl content based on the ECD spectra of known isoaspartyl/aspartyl mixtures of synthetic peptides. The observed linearity appears to be sequence independent because the relationship exists despite sequence variations and changes in backbone fragment abundances when isoaspartyl and aspartyl residues are interchanged. Furthermore, a new method to calculate the relative abundances of isomer from protein deamidation without synthetic peptides is proposed and tested using a linear peptide released by protein digestion that contains the deamidation site. The proteolytic peptide can be rapidly aged to the expected 3:1 (isoaspartyl:aspartyl) mixture to generate a two-point calibration standard for ECD analysis. The procedure can then be used to determine the relative abundance of deamidation products from in vivo or in vitro protein aging experiments.

Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Publishing Authors By Initials

JJ Cournoyer,C Lin,MJ Bowman,PB O'Connor,

For similar investigative techniques: chemistry, analytical: photometry: spectrophotometry: spectrophotometry, infrared: spectroscopy, fourier transform infrared research abstracts see: investigative techniques: chemistry, analytical: photometry: spectrophotometry: spectrophotometry, infrared: spectroscopy, fourier transform infrared research

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Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of the American Society for Mass Spectrome

VOLUME: 18

Page Numbers: 48-56

Journal Abbreviation: J. Am. Soc. Mass Spectrom.

ISSN: 1044-0305

DAY: 25

MONTH: 09

YEAR: 2006

Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Information

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LANGUAGE: eng

NlmUniqueID: 9010412

Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Keywords Mesh Terms:

KEYWORDS: Spectroscopy, Fourier Transform Infrared

MESH TERMS: methods

Chemical & Substance for Abstract: Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation. Information

Substance Name: Cytochromes c

Registry Number: 9007-43-6

Grant and Affiliation Information for Quantitating the relative abundance of isoaspartyl residues in deamidated proteins by electron capture dissociation.

AFFILIATION: Department of Chemistry, Boston University, Boston, Massachusetts, USA.

Country: United States

AGENCY: United States NCRR

GRANT: P41RR10888

ACRONYM: RR

MEDLINETA: J Am Soc Mass Spectrom

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