1H NMR sequential assignments and secondary structure analysis of human fibrinogen gamma-chain C-terminal residues 385-411.
1H NMR sequential assignments and secondary structure analysis of human fibrinogen gamma-chain C-terminal residues 385-411.
复制标题
人纤维蛋白原 γ 链 C 端残基 385-411 的 1 H NMR 顺序分配和二级结构分析。
DOI：
10.1021/bi00465a019
复制
发表时间：
1990
期刊：
影响因子：
2.9
通讯作者：
Kloczewiak,M
中科院分区：
文献类型：
--
作者：
Mayo,KH;Burke,C;Lindon,JN;Kloczewiak,M
Materials and MethodsHuman fibrinogen (Kabi, Sweden) was used without any further purification. Preparation of carboxymethylatedy-chain, degradation of the-chain with cyanogen bromide, and gel filtration chromatography of the-chain fragments on Sephadex G-50 columns were carried out as previously de-scribed (Kloczewiak et al., 1982) by using a Vydac C18, 300-Á, 1 X 25 cm column. A linear acetonitrile gradient from 5 to 40% was used in all runs; 0.05% trifluoroacetic acid was added to both the water and acetonitrile reservoirs. The desired peptide was eluted at approximately 12% acetonitrile and was concentrated by freeze-drying. The concentration was determined by standard amino acid analysis of the sample hydrolyzed with 6 Nhc1 at 150 C for 40 min. Identity of the peptide was confirmed by amino acid analysisand amino-terminal sequencing (gas phase; Applied Bioscience auto-matic sequencer).
