Boluda L, Alonso C, Fernández-Caldas E
Research and Development C.B.F. LETI, S.A. Madrid, Spain.
J Allergy Clin Immunol. 1998 Feb;101(2 Pt 1):210-6. doi: 10.1016/S0091-6749(98)70385-9.
The inhalation of olive (Olea europaea) pollen is an important cause of allergic respiratory diseases in southern Europe and California.
The aims of this study were to characterize the allergenic composition of O. europaea pollen collected in California and to purify two important allergens.
One hundred grams of O. europaea pollen was extracted dialyzed in 10 kd cut-off membranes and lyophilized. Allergen characterization was done by sodium dodecylsulfate-polyacrylamide gel electrophoresis and immunoblotting. Two allergens were isolated by gel filtration, ion exchange, and hydrophobic interaction chromatography and sequenced.
Ole e 4 has an apparent molecular weight, under reducing conditions, of 32 kd and pIs between 4.65 and 5.1. The N-terminal was blocked and the analysis of the amino acid sequence of two internal regions revealed no homology with other known proteins. Ole e 5 has a molecular weight of 16 kd and pIs between 5.1 and 6.5. The amino acid sequence of the N-terminal showed a high degree of homology with superoxide dismutase of several plant species. Ole e 4 and Ole e 5 had an IgE binding frequency by immunoblot of 80% and 35%, respectively.
Olive pollen extracts have a heterogeneous composition, with several important allergens. One of these allergens showed a high degree of homology with a superoxide dismutase.
在欧洲南部和加利福尼亚，吸入油橄榄（油橄榄属）花粉是过敏性呼吸道疾病的一个重要病因。
本研究旨在鉴定在加利福尼亚采集的油橄榄花粉的变应原组成，并纯化两种重要的变应原。
将100克油橄榄花粉进行提取，用截留分子量为10kd的透析袋透析，然后冻干。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和免疫印迹法对变应原进行鉴定。通过凝胶过滤、离子交换和疏水相互作用色谱法分离两种变应原并进行测序。
在还原条件下，油橄榄素4的表观分子量为32kd，等电点在4.65至5.1之间。其N端封闭，对两个内部区域的氨基酸序列分析显示与其他已知蛋白质无同源性。油橄榄素5的分子量为16kd，等电点在5.1至6.5之间。N端的氨基酸序列与几种植物的超氧化物歧化酶具有高度同源性。通过免疫印迹法，油橄榄素4和油橄榄素5的IgE结合频率分别为80%和35%。
油橄榄花粉提取物成分不均一，含有几种重要的变应原。其中一种变应原与超氧化物歧化酶具有高度同源性。
