Leukemia inhibitory factor and its receptor

Abstract

Publisher Leukemia inhibitory factor (LIF) appeared to be an extremely stable molecule and retained activity after treatment with strong denaturants extremes of pH (2–10) and temperature so long as the disulfide bonds remained intact. LIF was sensitive, however, to strong oxidizing conditions and conditions that allowed modification of free amino groups. Structural predictions based on the amino acid sequence of LIF had suggested that it would have a conformation similar to the long-chain 4-α-helical cytokines, growth hormone (GH), and granulocyte colony stimulating factor. The recent crystallization and X-ray structure determination of murine LIF has confirmed this prediction. Under normal ..