Quantitative Determination of Collagen Cross-links

羟赖氨酸 赖氨酰氧化酶 桥粒碱 化学 氧化脱氨基 赖氨酸 阿玛多利重排 交叉连接 糖基化 脱氨基 生物化学 戊糖苷 胺气处理 弹性蛋白 氨基酸 有机化学 细胞外基质 聚合物 生物 受体 遗传学
作者
Nicholas C. Avery,Trevor J. Sims,Allen J. Bailey
出处
期刊:Methods in molecular biology [Springer Science+Business Media]
卷期号:: 103-121 被引量:105
标识
DOI:10.1007/978-1-59745-413-1_6
摘要

The primary functional role of collagen is as a supporting tissue and it is now established that the aggregated forms of the collagen monomers are stabilised to provide mechanical strength by a series of intermolecular cross-links. In order to understand the mechanical properties of collagen, it is necessary to identify and quantitatively determine the concentration of the cross-links during their changes with maturation, ageing and disease. These cross-links are formed by oxidative deamination of the ε-amino group of the single lysine or hydroxylysine in the amino and carboxy telopeptides of collagen by lysyl oxidase, the aldehyde formed reacting with a specific lysine or hydroxylysine in the triple helix. The divalent Schiff base and keto-amine bonds so formed link the molecules head to tail and spontaneously convert during maturation to trivalent cross-links, a histidine derivative and cyclic pyridinolines and pyrroles, respectively. These latter bonds are believed to be transverse inter-fibrillar cross-links, and are tissue rather than species specific. We describe the determination of these cross-links in detail. Elastin is also stabilised by cross-linking based on oxidative deamination of most of its lysine residues to yield tetravalent cross-links, desmosine and iso-desmosine, the determination of which is also described. A second cross-linking pathway occurs during ageing (and to a greater extent in diabetes mellitus) involving reaction with tissue glucose. The initial product glucitol-lysine can be determined as furosine and pyridosine, and determination of advanced glycation end-products believed to be cross-links, such as pentosidine, are also described.
最长约 10秒,即可获得该文献文件

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
PDF的下载单位、IP信息已删除 (2025-6-4)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
萧水白应助liberty采纳,获得10
刚刚
1秒前
pipi发布了新的文献求助10
2秒前
3秒前
zhouz发布了新的文献求助10
4秒前
4秒前
小北完成签到,获得积分10
6秒前
6秒前
独特冰安发布了新的文献求助10
6秒前
一杯沧海完成签到 ,获得积分10
6秒前
8秒前
李健应助寡核苷酸小白采纳,获得10
8秒前
慕青应助shinn采纳,获得10
9秒前
LuckyJ_Jia发布了新的文献求助10
9秒前
9秒前
Ashley完成签到,获得积分10
9秒前
YifanWang应助wss123456采纳,获得20
10秒前
YifanWang应助wss123456采纳,获得20
10秒前
七堇发布了新的文献求助10
10秒前
12秒前
13秒前
刘子发布了新的文献求助10
13秒前
含蓄的金鱼完成签到,获得积分10
13秒前
所所应助直率谷蕊采纳,获得10
13秒前
怡然小夏完成签到,获得积分10
16秒前
16秒前
完美世界应助七堇采纳,获得10
17秒前
17秒前
琪凯定理发布了新的文献求助10
18秒前
19秒前
20秒前
酋长家大母鹅完成签到,获得积分10
22秒前
22秒前
ding应助vialavilda采纳,获得10
23秒前
源老头完成签到,获得积分10
23秒前
Xwu发布了新的文献求助10
24秒前
25秒前
万能图书馆应助BL采纳,获得10
25秒前
隐形曼青应助激昂的亦瑶采纳,获得10
25秒前
25秒前
高分求助中
Picture Books with Same-sex Parented Families: Unintentional Censorship 700
ACSM’s Guidelines for Exercise Testing and Prescription, 12th edition 500
Nucleophilic substitution in azasydnone-modified dinitroanisoles 500
不知道标题是什么 500
Indomethacinのヒトにおける経皮吸収 400
Phylogenetic study of the order Polydesmida (Myriapoda: Diplopoda) 370
Effective Learning and Mental Wellbeing 300
热门求助领域 (近24小时)
化学 材料科学 医学 生物 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 遗传学 基因 物理化学 催化作用 冶金 细胞生物学 免疫学
热门帖子
关注 科研通微信公众号,转发送积分 3975339
求助须知:如何正确求助?哪些是违规求助? 3519670
关于积分的说明 11199199
捐赠科研通 3256002
什么是DOI,文献DOI怎么找? 1798043
邀请新用户注册赠送积分活动 877386
科研通“疑难数据库(出版商)”最低求助积分说明 806305