Thorpe S C, Kemeny D M, Panzani R C, McGurl B, Lord M
Department of Medicine, UMDS, Guy's Hospital, London, England.
J Allergy Clin Immunol. 1988 Jul;82(1):67-72. doi: 10.1016/0091-6749(88)90053-x.
Castor bean proteins were separated and identified by isoelectric focusing and sodium dodecyl sulfate-polyacrylamide gel electrophoresis and blotted onto nitrocellulose paper. The capacity of the castor bean proteins to bind human IgE was probed with sera from castor bean-sensitive patients and radiolabeled anti-IgE. It proved difficult to identify allergens with isoelectric focusing. However, three allergens were identified when proteins were first separated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis: the 2S storage albumin, the 11S crystalloid proteins, and a third protein doublet with molecular weights of 47 and 51 kd. Specific IgE antibody to the 2S storage albumin, measured by RAST, was detected in most (96%) castor bean-sensitive patients, confirming it as the major allergen. We would like to suggest that the 2S albumin be named Ric c I, that the crystalloid proteins be named Ric c II, and that the 47/51 kd doublet be named allergen 3.
通过等电聚焦和十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳对蓖麻籽蛋白进行分离和鉴定，然后将其印迹到硝酸纤维素纸上。用来自蓖麻籽敏感患者的血清和放射性标记的抗IgE来检测蓖麻籽蛋白与人IgE结合的能力。事实证明，通过等电聚焦鉴定过敏原很困难。然而，当蛋白质首先在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳上分离时，鉴定出了三种过敏原：2S储存白蛋白、11S晶体蛋白和第三种分子量为47和51kd的蛋白双峰。通过放射变应原吸附试验（RAST）检测，大多数（96%）蓖麻籽敏感患者体内都检测到了针对2S储存白蛋白的特异性IgE抗体，证实其为主要过敏原。我们建议将2S白蛋白命名为Ric c I，将晶体蛋白命名为Ric c II，将47/51kd双峰命名为过敏原3。
