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Purification and Characterization of Bovine Placental Retinol-Binding Protein^*

Department of Animal Science, University of Tennessee (K.H.L., G.A.B., J.D.G.) Knoxville, Tennessee 37901
Department of Microbiology, University of Illinois (P.M.G.) Urbana, Illinois 61801

Address all correspondence and requests for reprints to: Dr. James D. Godkin, Department of Animal Science, University of Tennessee, Knoxville, Tennessee 37901.

Abstract

A major low mol wt acidic protein, 3B3, produced from cultures of day 29-90 bovine allantoic membranes (in the presence of [3H]leucine or [35S]methionine) and from day 29-60 allantoic fluid, has been purified. The protein consisted of three isoelectric variants (pi 5.3-6.1) of identical mol wt (23,200 ± 900) when analyzed by two-dimensional sodium dodecyl sulfatepolyacrylamide gel electrophoresis.

Amino-terminal sequence analysis of 3B3 isolated from allantoic fluid on the first 43 amino acids showed that 3B3 had 93% and 91% homology with rabbit and human plasma retinolbinding protein (RBP), respectively. The UV absorption spectrum and the fluorescence excitation and emission spectra of purified 3B3 from both sources indicated the presence of bound retinol. Rabbit antiserum was raised against placental RBP (3B3) isolated from allantoic membrane culture medium. Placental RBP was immunoprecipitated from radiolabeled allantois and chorion culture medium and was detected in allantoic membrane culture medium and allantoic fluid by Western blotting. These results suggested that bovine placental membranes secrete RBP into allantoic fluid and that placental RBP may play important roles in vitamin A metabolism in the developing embryo. (Endocrinology 127: 2696–2704, 1990)

Footnotes

^* This work was supported in part by USDA Grant 88-37242-4012, the Center of Excellence Program in Livestock Diseases and Human Health, College of Veterinary Medicine, and the Tennessee Agricultural Experiment Station, the University of Tennessee, Knoxville.

Received June 4, 1990.

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