Singh V, Curtiss R
Institute of Self-Organizing Systems and Biophysics, North-Eastern Hill University, Meghalaya, India.
Biochem Int. 1991 Oct;25(3):531-6.
In order to synthesize a bioeffective hormonotoxin for selective targeting to specific cells in the gonads, gelonin, a single chain ribosome-inactivating protein obtained from an Indian plant called Gelonium multiflorum was covalently linked to ovine luteinizing hormone (oLH) by a disulfide bond. Ovine LH-S-S-gelonin conjugates of different molar ratios were subjected to determine the ribosome-inactivating property in a cell-free translation assay using rabbit reticulocyte lysate system. A single amino group modification with N-succinimidyl-3-(2-pyridyldithio)propionate resulted in a loss of 90% protein synthesis inhibition activity. Upon conjugation of gelonin to oLH, the activity was further inhibited ranging from 2.5-6.4%. A 1:1 to 1:1.5 molar ratio (oLH-S-S-gelonin) conjugates showed 2.5-4.6% activity while 1:2.8 to 1:2.2 molar ratio exhibited 5.5-6.4% inhibition ability.
为了合成一种生物活性激素毒素，用于选择性靶向性腺中的特定细胞，从一种名为多花锡兰藤的印度植物中获得的单链核糖体失活蛋白gelonin，通过二硫键与绵羊促黄体生成素（oLH）共价连接。对不同摩尔比的绵羊LH-S-S-gelonin缀合物进行检测，以使用兔网织红细胞裂解物系统的无细胞翻译试验来确定核糖体失活特性。用N-琥珀酰亚胺基-3-（2-吡啶基二硫代）丙酸进行单氨基修饰导致蛋白质合成抑制活性丧失90%。当gelonin与oLH缀合时，活性进一步受到抑制，范围为2.5-6.4%。1:1至1:1.5摩尔比（oLH-S-S-gelonin）的缀合物显示出2.5-4.6%的活性，而1:2.8至1:2.2摩尔比表现出5.5-6.4%的抑制能力。
