Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain.
Factor XKetchikan: a variant molecule in which Gly replaces a Gla residue at position 14 in the light chain.
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XKetchikan 因子：一种变异分子，其中 Gly 取代了轻链 14 位的 Gla 残基。
DOI：
10.1007/bf00209404
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发表时间：
1995
期刊：
影响因子：
5.3
通讯作者：
James,HL
中科院分区：
文献类型：
--
作者：
Kim,DJ;Thompson,AR;James,HL
为寻找凝血因子X血浆促凝活性缺陷患者可能的分子缺陷，对凝血因子X基因外显子和剪接点进行异源双链分析和测序。外显子2中的突变被确认为在核苷酸位置206处A被G取代，编码Gly而不是Glu，Glu是氨基酸位置14处γ-羧基化谷氨酸（Gla）的正常前体。使用废除的TaqI限制性位点来指示缺陷的纯合性，但不能排除基因缺失和伴随的杂合性的发生。Gla残基的缺失可能影响因子X的Ca 2+结合特性或赋予干扰轻链相互作用特性的柔性。该缺陷可以解释先证者循环因子X功能活性降低和轻度出血倾向。
To seek the possible molecular defect in a patient with deficient factor X plasma procoagulant activity, factor X gene exons and splice junctions were subjected to heteroduplex analyses and sequencing. A mutation in exon 2 was confirmed as substitution of A by G at nucleotide position 206, coding for Gly instead of a Glu which is a normal precursor for γ-carboxylated glutamic acid (Gla) at amino acid position 14. An abolishedTaqI restriction site was used to indicate homozygosity of the defect, but occurrence of a gene deletion with attendant heterozygosity could not be excluded. The deletion of a Gla residue could affect the Ca2+-binding properties of factor X or confer a flexibility interfering with the interactive properties of the light chain. The defect could explain the decreased functional activity of circulating factor X and the mild bleeding tendency of the propositus.