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Molecular Cloning and Analysis of Functional cDNA and Genomic Clones Encoding Bovine Cellular Retinoic Acid-Binding Protein
Huda E. Shubeita, Joseph F. Sambrook and Anne M. McCormick
Proceedings of the National Academy of Sciences of the United States of America
Vol. 84, No. 16 (Aug. 15, 1987), pp. 5645-5649
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/30096
Page Count: 5
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A recombinant cDNA clone, pCRABP-HS1, encoding cellular retinoic acid-binding protein was isolated from a bovine adrenal cDNA library. COS-7 cells transfected with pCRABP-HS1 produced a biologically active retinoic acid-binding protein molecule of the expected molecular mass (15.5 kDa). RNA blot hybridization analysis using pCRABP-HS1 as a probe revealed a single 1050-nucleotide mRNA species in bovine adrenal, uterus, and testis, tissues that contain the highest levels of retinoic acid-binding activity. No hybridization was detected in RNA extracted from ovary, spleen, kidney, or liver, which contain relatively low levels of cellular retinoic acid-binding protein activity. Analysis of genomic clones isolated from an EcoRI* bovine genomic library demonstrated that the bovine cellular retinoic acid-binding protein gene is composed of four exons and three introns. Two putative promoter sequences were identified in the cloned 5′ sequence of the gene.
Proceedings of the National Academy of Sciences of the United States of America © 1987 National Academy of Sciences