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  • Title: Partial purification and characterization of a neutral insulin-like growth factor. Biochemical and biological properties.
    Author: Minuto F, Barreca A, Del Monte P, Giordano G.
    Journal: Biochem Int; 1986 Aug; 13(2):253-61. PubMed ID: 3768011.
    Abstract:
    A peptide with an isoelectric point of 6.5-7.0 was purified from Cohn fraction IV on the basis of its capacity to cross react with labelled insulin to human placental cell membrane receptors. It possesses insulin-like activity in the adipocyte bioassay (30 mU insulin equivalent/mg of protein) which is in the same order as its activity in the insulin radioreceptorassay (25.5 mU/mg). Somatomedin bioactivity is 40 U/mg in the porcine cartilage assay. In contrast, although in quiescent human fibroblast this peptide preparation has 6% of the mitogenic potency of somatomedin-C/insulin-like growth factor I on a weight basis, cross-reactivity in radioimmunoassay for somatomedin-C/insulin-like growth factor I, insulin-like growth factor II and insulin are very low. It is concluded that this peptide, although exhibiting the major biological characteristics of an insulin-like growth factor is different from the hitherto described somatomedins.
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