Synthetic rat, human, bovine/caprine, porcine and ovine growth hormone-releasing factor (GRF) were tested for their capacity to release growth hormone (GH) by the rat anterior pituitary in vitro. All peptides elicited parallel and dose-dependent increases in GH release and produced similar maximal GH secretion. Rat GRF was 3-6 times more potent in stimulating the release of GH than all other GRFs, while human, bovine/caprine, porcine and ovine GRF had potencies that were not statistically different. The increased potency of both rat GRF(1-27)NH2 and rat GRF(1-23)NH2 when compared to human GRF(1-27)NH2 and human GRF(1-23)NH2, respectively, suggests that the increased potency of this molecule resides in structural differences in the amino terminal of native GRF. The results demonstrate increased sensitivity of rat pituitary cells for their homologous releasing factor.