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βB2-晶体蛋白被葡萄糖和果糖糖基化的位点。

Sites of glycation of beta B2-crystallin by glucose and fructose.

作者信息

Zhao H R, Smith J B, Jiang X Y, Abraham E C

机构信息

Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912-2100, USA.

出版信息

Biochem Biophys Res Commun. 1996 Dec 4;229(1):128-33. doi: 10.1006/bbrc.1996.1768.

DOI:10.1006/bbrc.1996.1768
PMID:8954094
Abstract

We determined the sites of glycation of bovine beta B2-crystallin by glucose and fructose. After incubation with glucose or fructose, glycated tryptic peptides were purified by affinity chromatography/reverse-phase HPLC and identified by electrospray ionization mass spectrometry (ESIMS). The results gave evidence of glycation at lysine 10, 75, 100, 107, 120, 139, 167 and 171 by both glucose and fructose, while glycated lysine 119 and 47 or 67 were detected only after fructosylation. We conclude that glucose and fructose have similar glycation specificity.

摘要

我们确定了葡萄糖和果糖对牛βB2-晶体蛋白的糖基化位点。在与葡萄糖或果糖孵育后,通过亲和色谱/反相高效液相色谱法纯化糖化胰蛋白酶肽,并通过电喷雾电离质谱法(ESIMS)进行鉴定。结果表明,葡萄糖和果糖均可使赖氨酸10、75、100、107、120、139、167和171发生糖基化,而仅在果糖基化后才检测到糖化赖氨酸119以及47或67。我们得出结论,葡萄糖和果糖具有相似的糖基化特异性。

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引用本文的文献

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Adv Nutr. 2017 Jan 17;8(1):54-62. doi: 10.3945/an.116.013912. Print 2017 Jan.
2
Gamma III-crystallin is the primary target of glycation in the bovine lens incubated under physiological conditions.在生理条件下孵育的牛晶状体中,γIII-晶状体蛋白是糖基化的主要靶点。
Biochem J. 2003 Sep 15;374(Pt 3):677-85. doi: 10.1042/BJ20030542.