Simpson R J, Moritz R L, Rubira M R, Van Snick J
Joint Protein Structure Laboratory, Ludwig Institute for Cancer Research, Parkville, Victoria, Australia.
Eur J Biochem. 1988 Sep 1;176(1):187-97. doi: 10.1111/j.1432-1033.1988.tb14267.x.
Murine interleukin-HP1 (HP1) was originally identified as a T-cell-derived lymphokine with growth factor activity for B-cell hybridomas and plasmacytomas. This growth factor was recently shown to stimulate both normal B-cell differentiation and T-cell growth factor activity. We have determined the complete amino acid sequence of HP1 on 40 micrograms (approximately 2 nmol) protein using a combination of sensitive microbore column (1.0 and 2.1 mm internal diameter) HPLC, peptide mapping and automated amino acid microsequence analysis. Ion-pairing chromatography was employed to isolate hydrophilic peptides which were not retained on conventional reversed-phase HPLC systems. The molecule consists of 187 amino acid residues with a calculated molecular mass of 21710 Da. Although there is virtually no similarity between the NH2-terminal region of HP1 and its human biological counterpart (26-kDa protein/interferon-beta 2 = B-cell stimulatory factor-2/interleukin-6), these studies demonstrate extensive amino acid similarity in the middle and COOH-terminal regions of these molecules suggesting that HP1 is the murine homologue of human interleukin-6.
小鼠白细胞介素-HP1（HP1）最初被鉴定为一种T细胞衍生的淋巴因子，对B细胞杂交瘤和浆细胞瘤具有生长因子活性。最近发现这种生长因子能刺激正常B细胞分化和T细胞生长因子活性。我们使用灵敏的微径柱（内径1.0和2.1毫米）高效液相色谱、肽图谱分析和自动氨基酸微序列分析相结合的方法，确定了40微克（约2纳摩尔）蛋白质上HP1的完整氨基酸序列。采用离子对色谱法分离在传统反相高效液相色谱系统上不保留的亲水性肽。该分子由187个氨基酸残基组成，计算分子量为21710道尔顿。尽管HP1的NH2末端区域与其人类生物学对应物（26 kDa蛋白/干扰素-β2 = B细胞刺激因子-2/白细胞介素-6）几乎没有相似性，但这些研究表明这些分子的中部和COOH末端区域存在广泛的氨基酸相似性，这表明HP1是人类白细胞介素-6的小鼠同源物。
