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J. Biol. Chem., Vol. 266, Issue 23, 14978-14985, Aug, 1991
CO Bavik, U Eriksson, RA Allen and PA Peterson
We have developed a membrane binding assay by which we have been able to
characterize the interaction between 125I-labeled retinol-binding protein
and its receptor in microsome fractions derived from retinal pigment
epithelial cells. The binding of retinol-binding protein to the membranes
was fast, with a dissociation constant in the range of 31-72 nM, and
maximum binding occurred at neutral pH. Receptor binding sites were also
found in microsome fractions of liver and kidney, whereas lung and muscle
contained few, if any. Chemical cross-linking of retinol-binding protein to
the microsomal membranes yielded a major molecular complex of Mr 86,000
upon sodium dodecyl sulfate- polyacrylamide gel electrophoresis. The
protein responsible for binding of retinol-binding protein was identified
as a Mr 63,000 protein using a label transfer cross-linking technique.
Further characterization demonstrated that the receptor for retinol-binding
protein is a terminally glycosylated membrane protein noncovalently
associated with a high molecular weight complex.
Identification and partial characterization of a retinal pigment epithelial membrane receptor for plasma retinol-binding protein
Department of Immunology, Research Institute of Scripps Clinic, La Jolla, California 92037.
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