Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry-based amino acid analysis

Amino acid analysis has been an integral part of analytical biochemistry for more than 50 years. However, its experimental design, which includes derivatization of amino acids followed by some kind of chromatographic separation, has not changed over the years. We have developed a matrix-assisted las...

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Bibliographic Details
Published in:	Analytical biochemistry Vol. 335; no. 2; pp. 184 - 191
Main Authors:	Alterman, Michail A., Gogichayeva, Natalya V., Kornilayev, Boris A.
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 15-12-2004
Subjects:	Amino acid analysis Amino Acids - analysis Glucose Glucose - analysis Homocysteine MALDI-TOF Reproducibility of Results Serum Albumin, Bovine - analysis Serum Albumin, Bovine - chemistry Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization - methods Time Factors Glucose Amino acid analysis MALDI-TOF Homocysteine
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Summary:	Amino acid analysis has been an integral part of analytical biochemistry for more than 50 years. However, its experimental design, which includes derivatization of amino acids followed by some kind of chromatographic separation, has not changed over the years. We have developed a matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF)-based method for the quantitative analysis of amino acids. This method does not require any amino acid modification, derivatization, or chromatographic separation. The data acquisition time is decreased to several seconds for a single sample. No significant ion suppression effects were observed with the developed sample deposition technique, and the method was found to be reproducible. Linear responses between the amino acid concentration and the peak intensities ratio of corresponding amino acid to internal standard were observed for all amino acids analyzed in the range of concentrations from 20 to 300μM, and correlation coefficients were between 0.983 (for arginine) and 0.999 (for phenylalanine). Limits of quantitation were between 0.03μM (for arginine) and 3.7μM (for histidine and homocysteine). This method was applicable to the mixtures of free amino acids as well as to HCl hydrolysates of proteins. Furthermore, we have shown that this method can be applied to other biologically important low-molecular weight compounds such as glucose.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0003-2697 1096-0309
DOI:	10.1016/j.ab.2004.06.031