Metabolism of synthetic human heptadecapeptide gastrin by the isolated perfused rat liver.

Synthetic human heptadecapeptide gastrin-1 (SHG-17-1) and rat insulin were perfused cyclically through the isolated rat liver in a plasma-free medium. Synthetic human gastrin did not disappear from the medium at either physiological or supraphysiological levels, whereas rat insulin was cleared rapidly. Chromatography of perfusion samples showed that the SHG-17-U was neither lysed to smaller peptides nor changed to the larger molecular weight species. The isolated rat liver apparently plays no role in the metabolism of synthetic human heptadecapeptide gastrin-I.