Hybrid molecules of human growth hormone (GH) and porcine GH were cons
tructed using site-directed mutagenesis to obtain human GH mutants wit
h multiple (R8S, D11A, M14V, H18Q, R19H), (Y164S, R167K), (Y164S, R167
K, D171H) or single Y35S, R64A, or Q181 amino acid substitutions. When
tested with the Nb2 lymphoma cells, these substitutions had almost no
effect on the GH growth-promoting activity. However, GH binding to ce
ll receptors was altered.