By G.D. Aurbach and Donald B. McCormick (Eds.)
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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that IGFBP-2 had a 10- to 20-fold preferential affinity for IGFI1 when IGF-I1 tracer was used, although L. A. Bach (unpublished results) only saw a 5-t o 6-fold increase.
Thus, human IGFBP-6 lacks 2 and rat IGFBP-6 lacks 4 of the 18 cysteines in IGFBPs 1-5 respectively (Fig. IGFBP-6 does not contain an RGD sequence. Human (but not rat) IGFBP-6 contains a potential N-glycosylation site at its COOH terminus. , 1992b). , 1991), clusters of 0-glycosylated residues occur in serine-threonine-rich regions with nearby proline. Two such regions are found in the variable region (residues 117-128) and at the COOH terminus (residues 207-215) of human IGFBP-6. 20 MATTHEW M. 3 kb by Northern blotting.
One molecule of ALS binds to one molecule of IGFBP-3. Since IGFBP-3 also binds one molecule of IGF-I or IGF-11, this suggests that the 150-kDa complex is a ternary complex consisting of one molecule each of IGF-I (or IGF-111, IGFBP-3, and ALS. , 1989). 5. Formation of the Ternary Complex The requirements for forming the ternary complex were examined in reconstitution experiments using radiolabeled purified components, and monitored by affinity crosslinking (Baxter and Martin, 1989a). The ALS bound principally to IGF-I(IGF-II):IGFBP-3 complexes; only extremely weak interactions were observed between the ALS and IGFBP-3 in the absence of IGF-I or IGF-11.