Sugie M, Oka S, Tanaka H
Biomolecular Engineering Department, National Institute of Bioscience and Human-Technology, Ibaraki, Japan.
Biochem Biophys Res Commun. 1995 Oct 4;215(1):48-56. doi: 10.1006/bbrc.1995.2432.
Previous studies have shown that an Actinomycetes strain produces a novel protein with a molecular weight of 87,000 which stimulated the growth of murine erythroid progenitors in vitro, and we purified the protein. In this study, we have isolated and sequenced a clone encoding a polypeptide which had the equivalent activity. The clone contained an open reading frame of 334 amino acids. The activity was confirmed by the expression in E. coli as a fusion protein with glutathion S-transferase (GST). Based on the differences of molecular weight and N-terminal amino acid sequences, this protein was considered to be different from that previously reported and was named "ESA36".
先前的研究表明,一种放线菌菌株产生了一种分子量为87,000的新型蛋白质,该蛋白质在体外刺激了小鼠红系祖细胞的生长,并且我们纯化了该蛋白质。在本研究中,我们分离并测序了一个编码具有同等活性的多肽的克隆。该克隆包含一个334个氨基酸的开放阅读框。通过在大肠杆菌中作为与谷胱甘肽S-转移酶(GST)的融合蛋白表达来证实该活性。基于分子量和N端氨基酸序列的差异,该蛋白质被认为与先前报道的不同,并被命名为“ESA36”。