Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida).
Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida).
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从 Amphitrite ornata（多毛类、环节动物）的细胞外血红蛋白中分离含血红素的多肽链。
DOI：
10.1016/0305-0491(86)90283-x
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Bonaventura,C
中科院分区：
文献类型：
--
作者：
Fushitani,K;Bonaventura,J;Bonaventura,C
以二硫苏糖醇（DTT）为还原剂，经DE 52-纤维素离子交换层析，从文昌鱼（Amphitriterornata）胞外血红蛋白中分离出四条含血红素的多肽链，按洗脱顺序分别命名为AI、AII、BI和BII。链的NH 2-末端序列是AI，Asp-Ser-Asn-Ala; AII，Glu-Tyr-Thr; BI，Asp-Phe-Asn-Thr;和BII，Asp-Ser-Glu。每一个孤立的链显示光谱类似的脊椎动物血红蛋白，它们可逆地结合氧。酸性尿素聚丙烯酰胺凝胶电泳分离出四条带，对应于从DTT还原的完整细胞外血红蛋白中分离的链。这些结果和我们未能检测到相当数量的非血红素蛋白表明，A。ornata由四条多肽链组成，每条多肽链含有一个血红素。
From the extracellular hemoglobin of Amphitrite ornata four constituent polypeptide chains containing heme and designated AI, AII, BI and BII according to the elution order were obtained by DE52-cellulose ion-exchange chromatography with dithiothreitol (DTT) as a reducing reagent. The NH2-terminal sequences for the chains are AI, Asp-Ser-Asn-Ala; AII, Glu-Tyr-Thr; BI, Asp-Phe-Asn-Thr; and BII, Asp-Ser-Glu. Each of the isolated chains showed spectra similar to those of vertebrate hemoglobins, and they bound oxygen reversibly. Acid urea polyacrylamide gel electrophoresis separated four bands, corresponding to the isolated chain, from the intact extracellular hemoglobin reduced with DTT. These results and our failure to detect an appreciable amount of non-heme protein suggest that the extracellular hemoglobin of A. ornata is composed of four polypeptide chains, each containing a heme.