葡萄糖对αA-和αB-晶状体蛋白糖基化的位点选择性。
Site selectivity in the glycation of alpha A- and alpha B-crystallins by glucose.
作者信息
Abraham E C, Cherian M, Smith J B
机构信息
Department of Biochemistry and Molecular Biology, Medical College of Georgia, Augusta 30912.
出版信息
Biochem Biophys Res Commun. 1994 Jun 30;201(3):1451-6. doi: 10.1006/bbrc.1994.1866.
We determined the site selectivity of glycation by glucose (glucosylation) in alpha A- and alpha B-crystallins using two independent approaches. HPLC purified 14C-glucose labeled chymotryptic peptides and affinity chromatography/HPLC purified fully glycated peptides were identified by FAB-MS. Lys 11 and 78 of alpha A-crystallin and Lys 90 and/or 92 of alpha B-crystallin were the fast reacting sites of glucosylation.
我们使用两种独立的方法确定了葡萄糖（糖基化）对αA-和αB-晶状体蛋白的糖化位点选择性。通过FAB-MS鉴定了HPLC纯化的14C-葡萄糖标记的胰凝乳蛋白酶肽段以及亲和色谱/HPLC纯化的完全糖化的肽段。αA-晶状体蛋白的Lys 11和78以及αB-晶状体蛋白的Lys 90和/或92是糖基化的快速反应位点。
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