Document Type

Article

Date

1998

Embargo Period

11-29-2010

Keywords

Amino Acid Substitution, Animals, Arginine, Cloning Molecular, Escherichia coli, Eye Proteins/chemistry, Eye Proteins/metabolism, Eye Proteins/physiology, Gene Expression, Glutamine, Mutagenesis Site-Directed, Recombinant Fusion Proteins, Retinol-Binding Proteins/chemistry, Retinol-Binding Proteins/metabolism, Retinol-Binding Proteins/physiology, Stearic Acids/pharmacokinetics, Vitamin A/pharmacokinetics, Xenopus

Language

English

Disciplines

Chemistry

Description/Abstract

Interphotoreceptor retinoid-binding protein (IRBP) is unusual for a lipid-binding protein in that its gene is expressed uniquely by cells of photoreceptor origin and consists of four homologous repeats, each coding for a module of~300 amino acid residues. All-trans retinol binding domains, which appear to be present in each module, are composed of conserved hydrophobic regions [Baer et al, Exp Eye Res 1998; 66:249-262]. Here we investigate the role of highly conserved arginines contained in these regions.

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Chemistry Commons

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