Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P47989 (xanthine oxidase)
 8,633 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effect of mastitis on the milk fat globule membrane of milk samples from individual quarters was investigated. Wisconsin Mastitis Test positive (greater than 20mm) milk contained approximately 10% less milk fat globule membrane material than negative (smaller than 10mm) milk. The lipid portion of the milk fat globule membrane preparation from positive milk contained smaller amounts of phospholipids and larger amounts of cholesterol. Milk fat globule membrane preparations from positive milk had higher aldolase activity and lower xanthine oxidase activity. Dissociated membrane protein prepared from positive milk was resolved into five components by polyacrylamide gel electrophoresis while the membrane protein prepared from negative milk was resolved into three components.
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PMID:Influence of mastitis on properties of milk. XI. Fat globule membrane. 111 37

The aim of this paper is to apply inverse regression as a method for treating experimental data obtained from gel filtration chromatography in order to obtain estimates of hydrodynamic parameters of globular proteins with true confidence intervals. The method is illustrated with the determination, using inverse regression, of molecular mass and Stokes radius for four test proteins (aldolase, chymotrypsinogen A, aldehyde oxidase and xanthine oxidase), from experimental data obtained with a Sephacryl S-300 column. A simple personal computer (PC) program written in standard basic, that is useful for this purpose, is included.
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PMID:Application of inverse regression for estimating molecular masses and Stokes radii of globular proteins by gel filtration chromatography. 231 34

Sequential studies on levels of glycogen and lactic acid as well as activities of glucose-6-phosphatase, fructose-1, 6-diphosphatase aldolase, aspartic and ornithine transcarbamylase, arginase and xanthine oxidase were carried out in liver and tumour tissue of mice fed with 0.03% thioacetamide in normal stock diet. It was observed that significant decrease in glycogen content and activities of gluconeogenic enzymes was apparent at the age of 4 months, i.e. 2 months after thioacetamide treatment. Alterations in the other parameters studied were observed later, i.e. at the age of 9 months. Maximum changes were observed in the hepatomas, i.e. at the age of 17 months.
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PMID:Studies on progressive metabolic alterations in thioacetamide induced hepatocarcinogenesis. 431 41

Among progeny of a hybrid (Rana shqiperica x R. lessonae) x R. lessonae, 14 of 22 loci form four linkage groups (LGs): (1) mitochondrial aspartate aminotransferase, carbonate dehydratase-2, esterase 4, peptidase D; (2) mannosephosphate isomerase, lactate dehydrogenase-B, sex, hexokinase-1, peptidase B; (3) albumin, fructose-biphosphatase-1, guanine deaminase; (4) mitochondrial superoxide dismutase, cytosolic malic enzyme, xanthine oxidase. Fructose-biphosphate aldolase-2 and cytosolic aspartate aminotransferase possibly form a fifth LG. Mitochondrial aconitate hydratase, alpha-glucosidase, glyceraldehyde-3-phosphate dehydrogenase, phosphogluconate dehydrogenase, and phosphoglucomutase-2 are unlinked to other loci. All testable linkages (among eight loci of LGs 1, 2, 3, and 4) are shared with eastern palearctic water frogs. Including published data, 44 protein loci can be assigned to 10 of the 13 chromosomes in Holarctic Rana. Of testable pairs among 18 protein loci, agreement between Palearctic and Nearctic Rana is complete (125 unlinked, 14 linked pairs among 14 loci of five syntenies), and Holarctic Rana and Xenopus laevis are highly concordant (125 shared nonlinkages, 13 shared linkages, three differences). Several Rana syntenies occur in mammals and fish. Many syntenies apparently have persisted for 60-140 x 10(6) years (frogs), some even for 350-400 x 10(6) years (mammals and teleosts).
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PMID:Linkage groups of protein-coding genes in western palearctic water frogs reveal extensive evolutionary conservation. 928 85