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1ml blood); v = k[TTR-RBPretinolhlood' b A diffusion-controlled reaction (CONNORS 1990). cValue of k from Noy and Xu (1990a). umol PM lipids (COOK 1958). An additional assumption is that retinol is equally distributed between the outer and in the inner leaflets of the PM. 5 nmollg tissue; v = k[retinol]pm/out. dValue of k from Noy et al. (1995). v = k[retinol]pm/in where [retinol]pm/in was calculated as detailed in footnote c, above. e Lower limit of k calculated from the upper limit of the Kd (Table 3) and the kOf!

1988). These considerations raise the question of whether the carboxyl group of RA is protonated or negatively charged at physiological pH, and whether the self-association characteristics of RA affect the compound's ionization state. These questions were examined in a study that utilized the large spectral shift of the absorption maximum of RA upon protonation of the carboxyl end group to monitor the ionization behavior of RA in water (Noy 1992a). The concentration dependence of the pK of RA indicated that the CMC of this retinoid is lower than 111M.

Biochemistry 34:11928-11937 Katakura Y, Totsuka M, Ametani A, Kaminogawa S (1994) Tryptophan-19 of betalactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim Biophys Acta 1207:58-67 Kersten S, Pan L, Chambon P, Gronemeyer H, Noy N (1995a) Role of ligand in retinoid signaling: 9-cis-retinoic acid modulates the oligomeric state of the retinoid X receptor.

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