Lykkegård S
Acta Pathol Microbiol Scand C. 1980 Aug;88(4):179-85. doi: 10.1111/j.1699-0463.1980.tb00092.x.
Anti-mouse renin specific Fab fragment was labelled with 125I and repurified on an affinity-column with renin as ligand in order to eliminate Fab fragments with a damaged antibody combining site. The 125I-labelled Fab fragment, with addition of unlabelled Fab fragment, was administered in vivo to sialoadenectomized mice. The serum disappearance curve of the Fab fragments with the intact antibody combining site possessed two components with a half life of 120 min for the slowest component. The renin specific Fab fragments inhibited the enzymatic activity of renin with a KI-value of 5.5 +/- 1.5 x 10(-9) M, compatible with competitive inhibition. The same Fab fragments were able to inhibit 99% of the enzymatic active renin. The administration of the Fab fragments caused a 3-4 fold increase in the total concentration of plasma renin, but the enzymatic activity was inhibited. No decrease in blood pressure was demonstrated in the animals.
抗小鼠肾素特异性Fab片段用125I标记,并在以肾素为配体的亲和柱上重新纯化,以去除抗体结合位点受损的Fab片段。将125I标记的Fab片段与未标记的Fab片段一起体内给予唾液腺切除的小鼠。具有完整抗体结合位点的Fab片段的血清消失曲线有两个成分,最慢成分的半衰期为120分钟。肾素特异性Fab片段抑制肾素的酶活性,KI值为5.5±1.5×10(-9)M,符合竞争性抑制。相同的Fab片段能够抑制99%的酶活性肾素。给予Fab片段导致血浆肾素总浓度增加3至4倍,但酶活性受到抑制。在动物中未观察到血压下降。