苏氨酸-95被鉴定为正常人髓鞘碱性蛋白糖基化的主要位点。
The identification of threonine-95 as the major site of glycosylation in normal human myelin basic protein.
作者信息
Cruz T F, Wood D D, Moscarello M A
出版信息
Biochem J. 1984 Jun 15;220(3):849-52. doi: 10.1042/bj2200849.
Abstract
The enzymic transfer of N-acetylgalactosamine to myelin basic protein and that to peptides derived from basic protein were compared. Basic protein treated with pepsin and trypsin before glycosylation resulted in decreases of 7% and 23% in the amount of N-acetylgalactosamine transferred to the peptides respectively. However, digestion of basic protein had little effect on the sites glycosylated. It was found that Thr-95 was the major site for glycosylation in both the intact human basic protein and in the tryptic peptides.
摘要
比较了N-乙酰半乳糖胺向髓鞘碱性蛋白和从碱性蛋白衍生的肽的酶促转移。在糖基化之前用胃蛋白酶和胰蛋白酶处理碱性蛋白，导致转移到肽上的N-乙酰半乳糖胺量分别减少了7%和23%。然而，碱性蛋白的消化对糖基化位点影响很小。发现在完整的人碱性蛋白和胰蛋白酶肽中，苏氨酸-95都是主要的糖基化位点。
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