Titlebook: Retinoid Protocols; Christopher P. F. Redfern Book 1998 Springer Science+Business Media New York 1998

Obstacle

教唆

Expression and Mutagenesis of Retinol-Binding Proteinthe thyroxine-binding protein, known as transthyretin (TTR). This complex exists in equilibrium with free holo-RBP, which can then interact with a specific cell-surface receptor, thereby inducing the release of its retinol to the target cell. Thus, RBP possesses at least three molecular-recogmtion p

BILE

Interactions of Retinol-Binding Protein with Transthyretin and Its Receptore previously been used. Both these techniques require milligram quantities of the proteins and this sets limitations on the use of these techniques for the study of RBP-TTR interactions using recombinant proteins. The . expression system described in . does not readily produce milligram quantities o

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Detection of Conformational Changes in Cellular Retinoid-Binding Proteins by Limited Proteolysists technique is that the more exposed an amino-acid residue is to the solvent, the easier it 1s for a protease to cleave a peptide bond at that site (., .). Therefore, regions of a protein with an extended conformation, such as those found in large multidomain proteins, are better substrates for pro

高調(diào)

Presbyopia

可能性

Preparation of Polyclonal Antibodies to Retinoid Receptorsents in characterizing the molecular activities of the retinoid receptors (.). The use of a retinoid “X” receptor α (RXRα) antibody on Western blots contributed to the identification of the RXR ligand by detection of the receptor in fractions of whole-cell lysates that were able to bind the 9-. reti

preeclampsia

1064-3745 llowing the cloning of nuclear receptors or RARs reported in 1987 (Fig. 1). Important discoveries since then have shown how RARs work as all-trans retinoic ac- dependent heterodimers with related nuclear receptors for 9-cis retinoic acid called RXRs. This has stimulated the development of synthetic

歡笑

FIR