Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.1.3.5 (5'-nucleotidase)
 3,167 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The binding of rat 125I-labelled high-density lipoprotein (HDL) to rat kidney membranes was studied using HDL fractions varying in their apolipoprotein E content. The apolipoprotein E/apolipoprotein A-I ratio (g/g) in the HDL fractions ranged from essentially 0 to 1.5. All these HDL preparations showed the same binding characteristics. The saturation curves, measured at 0 degrees C in the presence of 2% bovine serum albumin, consisted of two components: low-affinity non-saturable binding and high-affinity binding (Kd about 40 micrograms of HDL protein/ml). Scatchard analyses of the high-affinity binding suggest a single class of non-interacting binding sites. These sites could be purified together with the plasma membrane marker enzyme 5'-nucleotidase. The binding of rat HDL to rat kidney membranes was not sensitive to high concentrations of EDTA, relatively insensitive to pronase treatment and influenced by temperature. The specific binding of rat HDL was highest at acid pH and showed an additional optimum at pH 7.5. On a total protein basis unlabelled rat VLDL competed as effectively as unlabelled rat HDL for binding of 125I-labelled rat HDL to partially purified kidney membranes. Rat LDL, purified by chromatography on concanavalin A columns and human LDL did not compete. Unlabelled human HDL was a much weaker competitor than unlabelled rat HDL and the maximal specific binding of 125I-labelled human HDL was only 10% of the value for 125I-labelled rat HDL.
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PMID:Specific saturable binding of rat high-density lipoproteins to rat kidney membranes. 300 85

The binding of human 125I-labeled HDL3 to purified rat liver and testis plasma membranes was studied. About 50-65% of the total HDL binding in these membranes was abolished by 1% bovine serum albumin in the incubation medium. The remaining albumin-insensitive binding sites, determined in the presence of albumin were associated with plasma membranes; a good correlation was found between the 125I-labeled HDL3 binding and the 5'-nucleotidase activities of the membrane fractions. The binding sites in these tissues were saturable, specific for HDL (not competed for by LDL) and had similar affinities for 125I-labeled HDL3 (Kd, 11.8 micrograms protein/ml for liver and 12.7 micrograms protein/ml for testis membranes); the maximum binding capacity of the testis membranes was higher (1.3 vs. 0.7 microgram protein/mg membrane protein). Egg phosphatidylcholine complexes of both human apolipoprotein A-I and apolipoprotein C's competed for the HDL-binding sites, but phosphatidylcholine vesicles alone did not. Chemical modification of the lysine and arginine residues of apolipoproteins did not affect the interaction of HDL3 with its binding sites. Despite the fact that the HDL-binding sites in these tissues are not specific for apolipoprotein A-I, they may have important physiological roles in lipid transport, as they appear to recognize apolipoprotein-phospholipid complexes.
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PMID:Characterization of high-density lipoprotein binding sites in rat liver and testis membranes. 647 54