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Journal of Endocrinology (1988) 118, 7-18       DOI: 10.1677/joe.0.1180007
© 1988 Society for Endocrinology
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The biological and structural characterization of specific serum binding proteins for the insulin-like growth factors

G. T. Ooi and A. C. Herington

Medical Research Centre, Prince Henry's Hospital, Melbourne, Australia 3004

RECEIVED 23 November 1987

INTRODUCTION: The insulin-like growth factors (IGFs) or somatomedins are a family of growth hormone (GH)-dependent polypeptides believed to mediate the mitogenic actions of GH. They have close structural homology with insulin, and express similar biological activities (Rinderknecht & Humbel, 1978a,b; Zapf, Froesch & Humbel, 1981; Humbel, 1984; Van Wyk, 1984). Two distinct, but chemically related, IGFs have been purified from human plasma: a basic (isoelectric point, pI 8·4) peptide, IGF-I (or somatomedin C), which shares 43% sequence homology with human proinsulin (Rinderknecht & Humbel, 1978a) and a neutral (pI 6·5) peptide, IGF-II, which has a 60% homology with IGF-I (Rinderknecht & Humbel, 1978b). Somatomedin A, previously thought to be a distinct IGF, has now been shown to be a deamidated form of IGF-I (Enberg, Carlquist, Jornvall & Hall, 1984). Various forms of both IGF-I and




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