Quick quantification of proteins by MALDI

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Title
Quick quantification of proteins by MALDI
Author(s)
S H Ahn; J W Kang; Jeong Hee Moon; K P Kim; S H Lee; M S Kim
Bibliographic Citation
Journal of Mass Spectrometry, vol. 50, no. 3, pp. 596-602
Publication Year
2015
Abstract
Previously, we reported that the matrix-assisted laser desorption ionization spectrum of a peptide became reproducible when an effective temperature was held constant. Using a calibration curve drawn by plotting the peptide-to-matrix ion abundance ratio versus the peptide concentration in a solid sample, a peptide could be quantified without the use of any internal standard. In this work, we quantified proteins by quantifying their tryptic peptides with the aforementioned method. We modified the digestion process; e.g. disulfide bonds were not cleaved, so that hardly any reagent other than trypsin remained after the digestion process. This allowed the preparation of a sample by the direct mixing of a digestion mixture with a matrix solution. We also observed that the efficiency of the matrix-to-peptide proton transfer, as measured by its reaction quotient, was similar for peptides with arginine at the C-terminus. With the reaction quotient averaged over many such peptides, we could rapidly quantify proteins. Most importantly, no peptide standard, not to mention its isotopically labeled analog, was needed in this method.
Keyword
MALDIprotein quantificatonquantification of hGHquantification of myoglobintryptic digestion
ISSN
1076-5174
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/jms.3567
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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