白蛋白丘奇湾：560位赖氨酸突变为谷氨酸——通过电喷雾电离质谱检测到的新突变

Albumin Church Bay: 560 Lys-->Glu a new mutation detected by electrospray ionisation mass spectrometry.

作者信息

Chua E K, Brennan S O, George P M

机构信息

Department of Pathology, Christchurch School of Medicine, New Zealand.

出版信息

Biochim Biophys Acta. 1998 Feb 17;1382(2):305-10. doi: 10.1016/s0167-4838(97)00147-7.

DOI:10.1016/s0167-4838(97)00147-7

PMID:9540802

Abstract

Albumin Church Bay is a fast migrating genetic variant of human serum albumin which, in a heterozygous subject, formed about 50% of the circulating albumin. Reversed phase peptide mapping and electrospray ionisation mass spectrometry (ESI-MS) indicated that the C-terminal CNBr peptide had decreased polarity associated with a 1 Da increase in mass. Subdigestion of this peptide with trypsin and chymotrypsin revealed that the increased mass was associated with the chymotrypsin fragment VEKCCKADDKETCF (555-568) which had a mass of 1791.1 compared to 1790.2 for its normal counterpart. Sequence analysis of PCR-amplified DNA indicated an A-->G mutation at position 98 of exon 13, which causes a point mutation of 560 Lys-->Glu and results in a 1 Da mass increase.

摘要

白蛋白丘奇湾是人类血清白蛋白的一种快速迁移的遗传变体，在杂合子个体中，它约占循环白蛋白的50%。反相肽图谱和电喷雾电离质谱（ESI-MS）表明，C末端溴化氰肽的极性降低，质量增加了1 Da。用胰蛋白酶和胰凝乳蛋白酶对该肽进行亚消化显示，质量增加与胰凝乳蛋白酶片段VEKCCKADDKETCF（555 - 568）有关，其质量为1791.1，而其正常对应片段的质量为1790.2。对PCR扩增的DNA进行序列分析表明，外显子13第98位发生A→G突变，导致560位赖氨酸→谷氨酸的点突变，质量增加1 Da。