Yoh M, Morinaga N, Noda M, Honda T
Department of Bacterial Infections, Osaka University, Japan.
Toxicon. 1995 May;33(5):651-7. doi: 10.1016/0041-0101(95)00002-4.
Thermostable direct hemolysin (TDH) produced by Vibrio parahaemolyticus was iodinated using chloramine T. The 125I-labeled TDH retained up to 80% of the activity of intact toxin. The binding of 125I-TDH to rabbit erythrocytes was inhibited by addition of nonlabeled TDH. The binding of 125I-TDH to rabbit erythrocytes was completed in the 1st or 2nd min of incubation at 37 degrees C in contrast to that at 4 degrees C. 125I-TDH, which cannot lyse horse erythrocytes as does intact TDH, bound to horse erythrocytes as to those of rabbit. The dissociation constants (KD) derived Scatchard plots were 2.85, 4.39, 4.33 and 5.35 x 10-8M for rabbit, horse, human and sheep erythrocytes, respectively. The lytic sensitivity of various erythrocytes to TDH showed no relationship to the binding capacity.
用氯胺T对副溶血性弧菌产生的耐热直接溶血素（TDH）进行碘化。125I标记的TDH保留了高达80%的完整毒素活性。加入未标记的TDH可抑制125I-TDH与兔红细胞的结合。与在4℃时相比，125I-TDH与兔红细胞的结合在37℃孵育的第1或第2分钟完成。与完整的TDH不同，不能溶解马红细胞的125I-TDH与马红细胞的结合情况和与兔红细胞的类似。从Scatchard图得出的兔、马、人及绵羊红细胞解离常数（KD）分别为2.85、4.39、4.33和5.35×10-8M。各种红细胞对TDH的溶血敏感性与结合能力无关。
