Berman J M, Chen T M, Sargent R, Buck S H, Shea P, Heminger E F, Broersma R J
Merrell Dow Research Institute, Cincinnati, OH 45215.
FEBS Lett. 1988 Sep 12;237(1-2):76-80. doi: 10.1016/0014-5793(88)80175-3.
Two analogs of rat atrial natriuretic factor, rANF7-28-NH2 and [Mpr7,Ala20,D-Arg27]rANF7-27-NH2, were prepared by the solid-phase method. These peptides had 2-fold and 7-fold less affinity, respectively, than rANF1-28 in binding to membranes prepared from cultured aortic smooth muscle cells, and both peptides were 5-fold less potent than rANF1-28 in relaxing serotonin-contracted rabbit aortic rings. rANF7-28-NH2 was rapidly degraded by rat kidney homogenates but [Mpr7,Ala20,D-Arg27]rANF7-27-NH2 had enhanced stability against rat kidney homogenate degradation. However, this in vitro stability did not translate into an extended duration of action in vivo.
通过固相法制备了两种大鼠心房利钠因子类似物，即rANF7 - 28 - NH₂和[Mpr7,Ala20,D - Arg27]rANF7 - 27 - NH₂。在与培养的主动脉平滑肌细胞制备的膜结合时，这些肽与rANF1 - 28相比，亲和力分别低2倍和7倍，并且在舒张血清素收缩的兔主动脉环方面，这两种肽的效力均比rANF1 - 28低5倍。rANF7 - 28 - NH₂被大鼠肾脏匀浆迅速降解，但[Mpr7,Ala20,D - Arg27]rANF7 - 27 - NH₂对大鼠肾脏匀浆降解的稳定性增强。然而，这种体外稳定性并未转化为体内作用持续时间的延长。
