Turpeinen U, Sipilä I, Anttila P, Karjalainen U, Kuronen B, Kalkkinen N, Ahola T, Stenman U H
Helsinki University Central Hospital, Finland.
Clin Chem. 1995 Apr;41(4):532-6.
We here report the characteristics of two rare alpha-chain hemoglobin (Hb) variants. The variants were found during quantification of HbA1c by cation-exchange HPLC with the Diamat glycohemoglobin analyzer. They were further characterized by isoelectric focusing and PolyCAT A cation-exchange chromatography. The structure of the abnormal Hbs was established by amino acid analysis after separation of the globin chains by reversed-phase chromatography, digestion with trypsin, separation of the peptides by reversed-phase chromatography, and amino acid sequencing. These studies showed that the two variants were Hb Broussais [alpha 90 (FG2)Lys-->Asn] and Hb Cemenelum [alpha 92 (FG4)Arg-->Trp].
我们在此报告两种罕见的α链血红蛋白（Hb）变体的特征。这些变体是在使用Diamat糖化血红蛋白分析仪通过阳离子交换高效液相色谱法对糖化血红蛋白A1c（HbA1c）进行定量分析时发现的。通过等电聚焦和聚阳离子A阳离子交换色谱法对它们进行了进一步表征。通过反相色谱法分离球蛋白链、用胰蛋白酶消化、再通过反相色谱法分离肽段以及氨基酸测序后进行氨基酸分析，确定了异常血红蛋白的结构。这些研究表明，这两种变体分别是布劳赛血红蛋白[α90（FG2）赖氨酸→天冬酰胺]和塞梅内卢姆血红蛋白[α92（FG4）精氨酸→色氨酸]。
