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新型β2-微球蛋白的纯化及完整氨基酸序列

Purification and complete amino acid sequence of novel beta 2-microglobulin.

作者信息

Odani H, Oyama R, Titani K, Ogawa H, Saito A

机构信息

Bio-dynamics Research Institute, Nagoya, Japan.

出版信息

Biochem Biophys Res Commun. 1990 May 16;168(3):1223-9. doi: 10.1016/0006-291x(90)91159-p.

Abstract

We have previously reported that novel beta 2-microglobulin (beta 2m) is a metabolite derived from beta 2m in ultrafiltrate of patients on long-term hemodialysis (LT-HD). Chromatofocusing showed the presence of at least two major novel beta 2m's with isoelectric points of 5.38 and 5.22. In the present study we purified one of major novel beta 2m's and determined the complete amino acid sequence. We demonstrate herein that the novel beta 2m has the same sequence as native beta 2m except for the 17th residue from the N-terminus which was identified as Asp instead of Asn in native beta 2m, suggesting a possible deamidation during LT-HD.

摘要

我们之前曾报道,新型β2-微球蛋白(β2m)是长期血液透析(LT-HD)患者超滤液中源自β2m的一种代谢产物。色谱聚焦显示存在至少两种主要的新型β2m,其等电点分别为5.38和5.22。在本研究中,我们纯化了其中一种主要的新型β2m,并确定了其完整的氨基酸序列。我们在此证明,新型β2m与天然β2m具有相同的序列,只是从N端起第17个残基在新型β2m中被鉴定为天冬氨酸(Asp),而在天然β2m中为天冬酰胺(Asn),这表明在长期血液透析过程中可能发生了脱酰胺作用。

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