We have developed a 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 peakintensities ratio of correspondingamino acid to internal standard were observed for all amino acids analyzed in the range of concentrations from 20 M to 300 M and correlation coefficients were between 0.983 for arginine to 0.999 for phenylalanine. Limit of quantitation varied from 0.03 M for arginine to 3.7 M for histidine and homocysteine. This method was applicable to the mixtures of free amino acids as well as HCl hydrolysates of proteins. Further, we have shown that this method can be applied to other biologically important low-molecular weight compounds like glucose.

File Number: 2004 FY 16 

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