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Retinol-Binding Proteins

1974
Publisher Summary This chapter discusses the methods of isolation, chemical nature, physical properties, biochemistry, and methods of assay of retinol-binding proteins (RBP). The discovery of the importance of vitamin A (retinol) and of the animal in preventing night blindness and maintaining normal growth of the animal body, in replacement of ...
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Calcium-Binding Proteins

Annual Review of Biochemistry, 1976
Calcium binding, which appears to be either specific or physiologically significant, has been reported for 70 norminally "different" proteins. First, I catalog these proteins. Only a few recent or general references can be cited. Those proteins that serve critical physiological functions or that may be regarded as chemical prototypes are discussed in ...
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Polypyrimidine-tract-binding protein: a multifunctional RNA-binding protein

Biochemical Society Transactions, 2008
PTB (polypyrimidine-tract-binding protein) is a ubiquitous RNA-binding protein. It was originally identified as a protein with a role in splicing but it is now known to function in a large number of diverse cellular processes including polyadenylation, mRNA stability and translation initiation.
Kirsty, Sawicka   +3 more
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Protein Filter Binding

2014
This protocol describes a method to monitor the binding of nucleic acid to protein, allowing the determination of the apparent affinity of a nucleic acid-protein interaction.
Sarah, Kolitz, Jon R, Lorsch
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Calcium Binding Proteins

2012
The role of Ca(2+) as a key and pivotal second messenger in cells depends largely on a wide number of heterogeneous so-called calcium binding proteins (CBP), which have the ability to bind this ion in specific domains. CBP contribute to the control of Ca(2+) concentration in the cytosol and participate in numerous cellular functions by acting as Ca(2+)
Matilde, Yáñez   +2 more
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Iron‐binding Proteins

Acta Paediatrica, 1989
Brock, J. H. (Department of Bacteriology and Immunology, Western Infirmary, Glasgow, UK). Iron‐binding proteins.The structure and properties of the iron‐binding proteins transferrin, lactoferrin and transferrin are reviewed. Transferrin and lactoferrin are structurally similar, consisting of a single polypetide chain and reversibly binding two iron ...
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Sulfatide-binding proteins

Chemistry and Physics of Lipids, 1986
Sulfatides (galactosyl ceramide-I3-sulfate) and other sulfated glycolipids are found in many tissues. The cell adhesion proteins laminin, thrombospondin, and von Willebrand factor bind specifically to sulfated glycolipids. Methods for characterizing the specificity of these interactions using surface-adsorbed glycolipids are reviewed.
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Oxysterol-Binding Proteins

2010
In eukaryotic cells, membranes of the late secretory pathway contain a disproportionally large amount of cholesterol in relation to the endoplasmic reticulum, nuclear envelope and mitochondria. At one extreme, enrichment of the plasma membrane with cholesterol and sphingolipids is crucial for formation of liquid ordered domains (rafts) involved in cell
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PLASMA RETINOL‐BINDING PROTEIN*

Annals of the New York Academy of Sciences, 1980
Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is known about the chemical structure, metabolism, and biological roles of RBP. RBP is a single polypeptide chain with molecular weight close to 20,000.
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