Analysis of hydroxylation and O-glycosylation on lysine sites in deer-hide gelatin.
10.19540/j.cnki.cjcmm.20201025.101
- Author:
Rui LIU
1
;
Shuo CAI
1
;
Ke-Xuan ZHAO
1
;
Meng-Tong JIANG
1
;
Yun-Feng ZHENG
2
;
Hao-Kun XU
3
;
Rong HOU
3
;
Yong HUANG
3
;
Ming ZHAO
2
;
Jin-Ao DUAN
2
Author Information
1. Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing University of Chinese Medicine Nanjing 210023, China School of Pharmacy, Nanjing University of Chinese Medicine Nanjing 210023, China Jiangsu Key Laboratory of Research and Development in Marine Bio-resource Pharmaceutics, Nanjing University of Chinese Medicine Nanjing 210023, China.
2. Jiangsu Collaborative Innovation Center of Chinese Medicinal Resources Industrialization, National and Local Collaborative Engineering Center of Chinese Medicinal Resources Industrialization and Formulae Innovative Medicine, Nanjing University of Chinese Medicine Nanjing 210023, China School of Pharmacy, Nanjing University of Chinese Medicine Nanjing 210023, China.
3. Guizhou Guangjitang Health Pharmaceutical Co., Ltd. Guiyang 550014, China.
- Publication Type:Journal Article
- Keywords:
deer-hide gelatin;
glycosylation;
hydroxylation;
lysine site;
modifications;
type Ⅰ collagen
- MeSH:
Animals;
Deer/metabolism*;
Gelatin;
Glycosylation;
Hydroxylation;
Lysine/metabolism*;
Protein Processing, Post-Translational;
Tandem Mass Spectrometry
- From:
China Journal of Chinese Materia Medica
2021;46(3):591-598
- CountryChina
- Language:Chinese
-
Abstract:
Nano-LC MS/MS was used to analyze trypsin digested deer-hide gelatin(DHG) samples, hydroxylation and O-glycosylation on lysine sites of DHG were comprehensive identified by using PEAKS Studio software. The sites, sorts and amounts of hydroxylation and O-glycosylation on Type Ⅰ collagen α1 chain(COL1 A1) and α2 chain(COL1 A2) of DHG were revealed. As a result, 5 284 peptides were identified from DHG samples, which were mainly from COL1 A1 and COL1 A2. Among these peptides, there were 449 peptides with hydroxylysine, 442 with galactosyl-hydroxylysine, 449 with glucosyl-galactosyl-hydroxylysine. The major modified sites of hydroxylation and O-glycosylation in DHG were shown as follow: α1-9 N and α2-5 N in N-telopeptides, α1-87, α1-174, α1-930, α2-87, α2-174, α2-933 in triple helix domain, and α1-16 C in C-telopeptides. These hydroxylation and O-glycosylation were correlated with the formation and stability of collagen molecules and collagen fibrils. It is feasible for the collagens and peptides dissolving from deer skin collagen fibrils under high temperature and pressure decocting, high temperature and pressure also might destroy inter-molecular covalent cross-linking and help those glycol-peptides formations. The present study provided ideas and strategies for the in-depth investigation on DHG chemical constituents, and showed good theoretical significance and application value.
