Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023890 (cirrhosis)
 42,195 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Identification of the material present in human serum which is responsible for inhibition of binding of desialylated glycoproteins to rat hepatocyte membranes was accomplished by means of affinity chromatography using Sephadex to which the galactose-specific lectin, Ricinus Communis Agglutinin (RCAI) was covalently bound. RCAI-Sephadex was capable of extraction of virtually all of the inhibitory activity from cirrhotic serum. The RCA I-bound inhibitory activity could be eluted with 0.05 M D-galactose. The D-galactose eluate when subjected to radioimmunoelectrophoresis against a number of specific antibodies to human serum glycoproteins produced arcs corresponding to alpha 1-acid glycoprotein, alpha2-macroglobulin, IgG, IgA, and IgM. In another experiment putative terminal galactosyl groups of desialylated glycoproteins in the D-galactose eluate from cirrhotic serum exposed to RCAI-Sephadex were labelled with tritiated borohydride after treatment with galactose oxidase. Subsequent gel electrophoresis showed peaks of radioactivity throughout the area of the gel corresponding to protein molecular weights of the 19 S, 7 S, and 4 S classes. It thus appears that a heterogeneous population of desialylated serum glycoproteins accounts for the inhibition of binding of desialylated glycoprotein to the hepatocyte membrane and that these desialylated glycoproteins are present in small amounts in normal human serum and in greatly increased quantities in serum from patients with cirrhosis.
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PMID:Serum inhibitors of desialylated glycoprotein binding to hepatocyte membranes. 10 Dec 52

Clearance of 0-100 mg/L concentrations of galactose from the blood depends on nutrient hepatic blood flow. We can measure such concentrations, which was not previously possible, by a continuous-flow method involving the use of galactose oxidase and peroxidase, the latter being coupled to a fluorogenic substrate, p-hydroxyphenylacetic acid. Interfering substances in the peroxidase reaction are removed by zinc/alkali precipitation. Sensitivity is maximized by using saturating concentrations of the enzymes and substrate. In prepared plasma test samples with galactose concentrations of 10, 40, 70, and 100 mg/L, the within-run CV's ranged from 2.1 to 8.6%, and day-to-day CV's from 2.2 to 17.2%, the largest CV's being for the 10 mg/L concentration. Normal subjects are shown to clear galactose more efficiently than subjects with moderate cirrhosis.
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PMID:Continuous-flow fluorometry of low galactose concentrations in blood or plasma. 735 77