High-Performance Liquid Chromatography/Mass Spectrometry Analysis Of Collagen Degradation Products
Keywords
Collagen, Enzymatic Hydrolysis, High Performance Liquid Chromatography, Mass Spectrometry
Abstract
High-performance liquid chromatography/mass spectrometry was used to analyze the polypeptide mixture obtained by denaturation and enzymatic hydrolysis of collagen II and I, and the differences between the two types of collagen degradation products were comparatively studied. Liquid chromatography-mass spectrometry was used to analyze the peptide mixture. Characteristic peptides in different types of collagen were identified. Collagen can be dissolved in salt solution after being treated at 50¡ãC for 3 hours. Gel filtration analysis results show that the molecular weight of thermally denatured collagen is more than 100,000. Therefore, the triple helix structure of collagen is destroyed during the thermal denaturation process but there is no obvious randomness. degradation. Collagen was digested with trypsin. When the enzyme dosage was 2%, pH 8.1~8.2, and temperature 37¡ãC, the collagen was completely degraded after 20 hours of treatment, and the average molecular weight of the polypeptide mixture was less than 10,000. The polypeptides in type II and type I collagen degradation products were studied using liquid mass spectrometry, and the sequences of the polypeptides in collagen degradation products were analyzed by multi-stage mass spectrometry. The results show that there are characteristic peptides of specific sequences in the polypeptide mixture after hydrolysis of different types of collagen, and it is feasible to use characteristic peptides to identify collagen types.
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Original research was done by Ni Wen, Sun Aimei, Zhang Guifeng, Su Zhiguo
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