Alenius H, Kalkkinen N, Lukka M, Turjanmaa K, Reunala T, Mäkinen-Kiljunen S, Palosuo T
National Public Health Institute, Helsinki, Finland.
Int Arch Allergy Immunol. 1995 Mar;106(3):258-62. doi: 10.1159/000236851.
We purified from natural rubber latex (NRL) by means of high-performance liquid chromatography a 27-kD protein, recognized characteristically by IgE in sera from latex-allergic children with spina bifida or other congenital anomalies and histories of multiple surgeries. N-terminal sequence analysis of the purified 27-kD protein was unsuccessful suggesting that its N-terminus is blocked. To obtain internal sequence information from the protein it was digested with trypsin and the purified tryptic peptides were subjected to sequence analysis. Thirteen of the 14 sequenced peptides revealed no significant homology to any of the published protein sequences indicating that the 27-kD protein is previously undescribed at the primary structure level. However, one of the 14 sequenced peptides showed significant homology to the rubber elongation factor, a 14.6-kD NRL protein. For the time being, the 27-kD NRL protein is the first molecularly characterized NRL allergen associated with defined clinical manifestations of latex allergy.
我们通过高效液相色谱法从天然橡胶胶乳（NRL）中纯化出一种27-kD蛋白，该蛋白在患有脊柱裂或其他先天性异常且有多次手术史的乳胶过敏儿童血清中可被IgE特异性识别。对纯化的27-kD蛋白进行N端序列分析未成功，提示其N端被封闭。为了获得该蛋白的内部序列信息，用胰蛋白酶对其进行消化，并对纯化的胰蛋白酶肽段进行序列分析。14个测序肽段中的13个与任何已发表的蛋白质序列均无明显同源性，表明该27-kD蛋白在一级结构水平上是此前未被描述过的。然而，14个测序肽段中的一个与橡胶延伸因子（一种14.6-kD的NRL蛋白）有明显同源性。目前，27-kD NRL蛋白是首个在分子水平上得到表征且与乳胶过敏特定临床表现相关的NRL过敏原。
