Watt K W, Cottrell B A, Strong D D, Doolittle R F
Biochemistry. 1979 Nov 27;18(24):5410-6. doi: 10.1021/bi00591a024.
The complete amino acid sequence of the alpha chain of human fibrinogen has been determined. It contains 610 amino acid residues and has a calculated molecular weight of 66,124. The chain has 10 methionines, and fragmentation with cyanogen bromide yields 11 peptides [Doolittle, R.F., Cassman, K.G., Cottrell, B.A., Friezner, S.J., Hucko, J.T., & Takagi, T. (1977) Biochemistry 16, 1703]. The arrangement of the 11 fragments was determined by the isolation of peptide overlaps from plasmic and staphylococcal protease digests of fibrinogen and/or alpha chains. In addition, certain of the cyanogen bromide fragments, preliminary reports of whose sequences have appeared previously, have been reexamined in order to resolve several discrepancies. The alpha chain is homologous with the beta and gamma chains of fibrinogen, although a large repetitive segment of unusual composition is absent from the latter two chains. The existence of this unusual segment divides the sequence of the alpha chain into three zones of about 200 residues each that are readily distinguishable on the basis of amino acid composition alone.
人纤维蛋白原α链的完整氨基酸序列已被确定。它含有610个氨基酸残基，计算分子量为66,124。该链有10个甲硫氨酸，用溴化氰裂解产生11个肽段[杜利特尔，R.F.，卡斯曼，K.G.，科特雷尔，B.A.，弗里兹纳，S.J.，胡科，J.T.，& 高木，T.（1977年）《生物化学》16卷，第1703页]。通过从纤维蛋白原和/或α链的血浆蛋白酶和葡萄球菌蛋白酶消化物中分离肽段重叠物来确定这11个片段的排列。此外，某些溴化氰片段（其序列的初步报告此前已出现）已被重新研究，以解决一些差异。α链与纤维蛋白原的β链和γ链同源，尽管后两条链中不存在一个由异常组成的大重复片段。这个异常片段的存在将α链的序列分成三个区域，每个区域约有200个残基，仅根据氨基酸组成就很容易区分。
