通过聚丙烯酰胺凝胶等电聚焦,在一个有争议的父权案件中发现了一个与DSaga相同的转铁蛋白D变异(DHR5)。

T Ohshima, T Takayasu, K Umetsu, M Fujita, C Satoh
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引用次数: 0

摘要

通过聚丙烯酰胺凝胶等电聚焦(PAGIF)在亲子鉴定病例的儿童中发现转铁蛋白(TF)变异。进一步的血清TF分析表明,这种罕见的TF变异遗传自所谓的父亲。通过PAGIF与几种已知的TF D变体进行直接比较,该TF变体被鉴定为TF DHR5,与变体TF DSaga相同。TF DHR5 (= DSaga)和TF C的全型(Fe(II)结合型)等电点(pi)分别为5.6和5.4。唾液酸酶处理后,TF DHR5 (= DSaga)比TF C在更基本的位置上出现了单条带迁移,这表明两者之间的pI差异是由于氨基酸取代造成的。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
A transferrin D variant (DHR5) identical with DSaga by polyacrylamide gel isoelectric focusing was found in a disputed paternity case.

A transferrin (TF) variant was found in the child in a paternity case by polyacrylamide gel isoelectric focusing (PAGIF). Further analysis of serum TF disclosed that this rare TF variant was inherited from the alleged father. This TF variant was identified as TF DHR5, being identical with a variant TF DSaga, in a direct comparison with several known TF D variants by PAGIF. The isoelectric points (pIs) of holo-type (Fe(II) binding type) of TF DHR5 (= DSaga) and TF C were 5.6 and 5.4, respectively. After sialidase treatment, TF DHR5 (= DSaga) showed a single band migrating at a more basic position than TF C, thus suggesting that the pI difference between the two was due to amino acid substitution.

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