Rosenberg E, Ravi Kiron M A, Soffer R L
Department of Biochemistry, Cornell University Medical College, New York, NY 10021.
Biochem Biophys Res Commun. 1988 Feb 29;151(1):466-72. doi: 10.1016/0006-291x(88)90616-x.
An angiotensin II-binding activity has been detected in the 100,000 x g supernatant fraction of rabbit liver. The total amount of binding activity in this fraction was substantially greater than that which could be solubilized from hepatic particles by treatment with digitonin. The crude soluble binding activity resembled the binding protein which had been purified from the particles in several respects. First, binding required the presence of p-chloromercuriphenylsulfonic acid and bound angiotensin II was released by dithiothreitol. Second, the molecular weight of the responsible protein cross-linked to radioiodinated angiotensin II was about 75,000 in the reduced, denatured state. Finally, guinea pig antiserum raised against the binding protein that had been purified from particles reacted identically with the soluble and solubilized activities.
在兔肝脏100,000×g超速离心上清液组分中检测到一种血管紧张素II结合活性。该组分中结合活性的总量显著高于用洋地黄皂苷处理从肝颗粒中溶解出的量。粗可溶性结合活性在几个方面类似于从颗粒中纯化的结合蛋白。首先，结合需要对氯汞苯磺酸的存在，且结合的血管紧张素II可被二硫苏糖醇释放。其次，在还原、变性状态下，与放射性碘标记的血管紧张素II交联的相关蛋白的分子量约为75,000。最后，针对从颗粒中纯化的结合蛋白产生的豚鼠抗血清与可溶性及溶解后的活性反应相同。
