Investigation on Identifying Collagen from Colla Corii Bovis Using Nano LC-MS/MS Method
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Graphical Abstract
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Abstract
OBJECTIVE To investigate the proteins and peptides in Colla Corii Bovis and indicate the possible modifications in Colla Corii Bovis by Shotgun based proteomics analysis. METHODS Trypsin was used to digest two batches of Colla Corii Bovis samples, and nano-LC Q Exactive Orbitrap mass spectrometry was applied to obtain the MS/MS spectra of Colla Corii Bovis digestion samples. Then PEAKS software was used to search those MS/MS spectra against Bovine protein database to identify peptides and proteins from Colla Corii Bovis samples. RESULTS As a result, totally 30 proteins and 1 378 peptides were identified, most of the peptides were derived from Collagen Ⅰ α1 chain, Collagen Ⅰ α2 chain, and Collagen Ⅲ α1 chain. In addition, there were four modifications indicated in the present study, including Hydroxylation, Deamidation, N-term Acetylation and Oxidation. CONCLUSION The material basis of Colla Corii Bovis was mainly from Collagen Ⅰ and Collagen Ⅲ, and those components after boiled, denatured, dissolved, and modified consist of the material basis of Colla Corii Bovis.
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