Esch R E, Klapper D G
Department of Microbiology and Immunology, University of North Carolina School of Medicine, Chapel Hill 27599.
Mol Immunol. 1989 Jun;26(6):557-61. doi: 10.1016/0161-5890(89)90007-2.
A series of peptides has been isolated from the Group I (GpI) allergen from five species of grasses currently under study in this laboratory. These peptides were generated by performing a limited tryptic digestion on each extensively reduced and alkylated GpI allergen and fractionating the digest by molecular sieve, ion-exchange and HPLC reverse-phase chromatography. Material in the elution profiles was assayed with a monoclonal antibody known to cross-react with all GpI allergens in this study. In addition, this particular monoclonal antibody has been previously shown to inhibit the ability of human IgE to bind to these GpI allergens. The peptides identified and isolated in this way were found to be highly homologous to one another.
从本实验室目前正在研究的五种禾本科植物的I组(GpI)变应原中分离出了一系列肽段。这些肽段是通过对每种充分还原和烷基化的GpI变应原进行有限的胰蛋白酶消化,并通过分子筛、离子交换和HPLC反相色谱对消化产物进行分级分离而产生的。用一种已知在本研究中能与所有GpI变应原发生交叉反应的单克隆抗体对洗脱图谱中的物质进行检测。此外,先前已证明这种特定的单克隆抗体能够抑制人IgE与这些GpI变应原结合的能力。以这种方式鉴定和分离出的肽段彼此高度同源。