In this study, histone H1, core histones H2A-H2B and H3-H4 were purified from chicken erythrocytes by hydroxylapatile chromatography. The nuclear extract was prepared from HeLa cells. We investigated the binding and interaction of histones and transcription factors on the upstream sequence of human autocrine motility factor receptor (hAMFR) gene by gel shift mobility assay. We found that the binding of H1 on the promoter sequence of hAMFR gene was relatively stable. We propose that H1 plays an important role in stablizing chromatosome. We also found that histones and HeLa cell extract could form a ternary complex with the DNA template.