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By G.D. Aurbach and Donald B. McCormick (Eds.)

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1990~)noted IGF-I1 tracer binding t o the 150kDa region using rat lymph. 111. BINDING PROPERTIES A. In most instances, IGF-I and IGF-I1 were bound with similar affinities (within a factor of 2) irrespective of whether IGF-I or IGF-I1 was the radioligand. The most notable exception to this generalization is human IGFBP-6, which had 60- to 70-fold greater affinity for IGF-I1 than IGF-I when IGF-I1 was used as tracer. Roghani et al. (1991) observed that IGFBP-2 had a 10- to 20-fold preferential affinity for IGFI1 when IGF-I1 tracer was used, although L.

The prepep- 18 MATTHEW M. RECHLER tide is 19 (rat) or 20 (human) residues long. Kiefer et al. (1991a) also isolated a human IGFBP-5 cDNA clone from a human osteosarcoma cDNA library. They noted that the NH, and COOH domains of IGFBP-5 and IGFBP-3 were more closely related than those of other IGFBF’s (50 and 45% identity, respectively). Rat IGFBP-5 mRNA is -6 kb on Northern blots (see below). The sequence of 1630 nucleotides of cDNA has been determined including the protein coding region, a 550-bp 5‘ untranslated region, and 264 bp of 3’ untranslated region without a poly(A) tract.

Human IGFBP-5 had a 3- to 10-fold higher apparent affinity for IGF-I1 than IGF-I using IGF-I1 tracer. The affinity of IGFBP-6 for IGF-11, 1-3 X 1011M - l, is higher than the affinity of other IGFBPs for IGF-I or IGF-11. Both IGFBP-6 and IGFBP-2 contribute to the preferential binding of IGF-I1 to human CSF (see below). , 1991). 1 L M Pg ND 33 290 100 440 15 17 -10 3 20 70 60 19 21 N Pg 0 G I P Pg Human (h), rat (r), bovine (b). A, Baxter et al. (1987); B, Busby et al. (1988b); C, Jones et al. (1991); D, Unterman et al.

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