Coscia M R, Ruffilli A, Oreste U
Institute of Protein Biochemistry and Enzymology, CNR, Naples, Italy.
Allergy. 1995 Nov;50(11):899-904. doi: 10.1111/j.1398-9995.1995.tb02496.x.
We describe a group of basic isoforms of Par o 1 (cumulatively referred to as Par o 1b), purified by anion-exchange chromatography. The allergenic activity of Par o 1b was compared with that of the acidic isoform (Par o 1a) by RAST inhibition. Par o 1b showed a cathodic mobility in crossed immunoelectrophoresis. It was found to be homogeneous in SDS-PAGE and SE-HPLC (14.5 kDa), and heterogeneous in PAG-IEF, yielding five IgE-binding bands with pI ranging between 7.9 and 9.6 PAG-IEF individual components were isolated by cation-exchange HPLC. The N-terminal amino acid sequence of the main component (pI 8.8) was determined and found to be similar to that of Par o 1a.
我们描述了一组通过阴离子交换色谱法纯化的Par o 1基本亚型(统称为Par o 1b)。通过RAST抑制法比较了Par o 1b与酸性亚型(Par o 1a)的致敏活性。Par o 1b在交叉免疫电泳中显示出阴极迁移率。发现其在SDS-PAGE和SE-HPLC中均一(14.5 kDa),而在PAG-IEF中不均一,产生五条IgE结合带,pI范围在7.9至9.6之间。通过阳离子交换HPLC分离PAG-IEF各个组分。测定了主要组分(pI 8.8)的N端氨基酸序列,发现其与Par o 1a的相似。