Add time:09/03/2019         Source:sciencedirect.com

Two analogs of rat atrial natriuretic factor, rANF7–28-NH2 and [Mpr7, Ala2O,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 [Mpr7Ala2O,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.

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