鸭卵抑素中硫酯位点周围32个残基区域的氨基酸序列。
Amino acid sequence of a 32-residue region around the thiol ester site in duck ovostatin.
作者信息
Nagase H, Brew K
机构信息
Department of Biochemistry, University of Kansas Medical Center, Kansas City 66103.
出版信息
FEBS Lett. 1987 Sep 28;222(1):83-8. doi: 10.1016/0014-5793(87)80196-5.
To obtain the amino acid sequence at the thiol ester site in duck ovostatin for comparisons with other proteins, the native ovostatin was labeled with 14CH3NH2 at the reactive thiol ester site. The modified protein was reduced, carboxymethylated, and digested with trypsin. 14C-labeled peptides isolated by gel filtration with Sephadex G-50, ion-exchange chromatography on DEAE-cellulose and HPLC were subjected to automated sequence analysis, and the stretch of 32 amino acid residues containing the 14CH3NH2-binding site were determined. A comparison of this sequence with the corresponding sequences in alpha 2-macroglobulin, and complement components C3 and C4 revealed 72, 31 and 34% homology, respectively. The results indicate that ovostatin is a close relative to plasma alpha-macroglobulins and may share a common ancestor with C3 and C4.
为了获得鸭抑卵素硫酯位点的氨基酸序列以便与其他蛋白质进行比较，天然抑卵素在反应性硫酯位点用¹⁴CH₃NH₂进行标记。修饰后的蛋白质经还原、羧甲基化处理，并用胰蛋白酶消化。通过用葡聚糖凝胶G - 50进行凝胶过滤、在二乙氨基乙基纤维素上进行离子交换色谱以及高效液相色谱分离得到的¹⁴C标记肽段，进行自动序列分析，确定了包含¹⁴CH₃NH₂结合位点的32个氨基酸残基的片段。将该序列与α₂ - 巨球蛋白以及补体成分C3和C4中的相应序列进行比较，分别显示出72%、31%和34%的同源性。结果表明，抑卵素与血浆α - 巨球蛋白关系密切，可能与C3和C4有共同的祖先。
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