MALDI-TOF 질량분석기를 이용한 소가죽과 물소가죽의 감별법
Identification of Bovine Leather and Water Buffalo Leather Using MALDI-TOF MS
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초록
This study was performed to develop a reliable method for identifying distinct animal species of finished leather products, using MALDI-TOF MS (matrix assisted laser desorption ionization-time of flight mass spectrometry). A series of leather samples from two different species of Bovidae, bovine (Bos taurus) and water buffalo (Bubalus bubalis), were used as controls to ensure the validity of the method. The samples were treated in 2-mercaptoethanol to destroy the disulfide bridges of the protein chains and were then digested with trypsin, an endoproteolytic enzyme, to cleave the protein chain into peptides containing lysine (K) and arginine (R) residues. The modified peptides were mixed with an HCCA matrix (α-cyano hydroxycinnamic acid) to form the sample/matrix composition. This mixture was then eluted onto a steel target plate and ionized by laser. The formed pool of cleaved peptides was measured by MALDI-TOF MS and arranged according to their molecular weight to charge ratio (m/z). The comparison of the mass spectra allowed the investigation of species-specific peaks between bovine and water buffalo leather. Traditional microscopic methods were used to verify consistency with the experimental values determined by MALDI-TOF MS
Abstract
This study was performed to develop a reliable method for identifying distinct animal species of finished leather products, using MALDI-TOF MS (matrix assisted laser desorption ionization-time of flight mass spectrometry). A series of leather samples from two different species of Bovidae, bovine (Bos taurus) and water buffalo (Bubalus bubalis), were used as controls to ensure the validity of the method. The samples were treated in 2-mercaptoethanol to destroy the disulfide bridges of the protein chains and were then digested with trypsin, an endoproteolytic enzyme, to cleave the protein chain into peptides containing lysine (K) and arginine (R) residues. The modified peptides were mixed with an HCCA matrix (α-cyano hydroxycinnamic acid) to form the sample/matrix composition. This mixture was then eluted onto a steel target plate and ionized by laser. The formed pool of cleaved peptides was measured by MALDI-TOF MS and arranged according to their molecular weight to charge ratio (m/z). The comparison of the mass spectra allowed the investigation of species-specific peaks between bovine and water buffalo leather. Traditional microscopic methods were used to verify consistency with the experimental values determined by MALDI-TOF MS
참고문헌 (14)
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