Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0155339 (Brown)
 12,436 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Eight yearling Holstein heifers (330 kg) were utilized in two 4 x 4 Latin squares. Diets were normal and brown midrib genotypes of Redlan x Greenleaf and Redlan x Piper varieties of ensiled first-cutting sorghum-sudangrass harvested at early head stage of maturity. Composition of hemicellulosic monosaccharides and alkali-soluble lignin phenolic compounds in feeds and corresponding digestibilities were estimated. Arabinose, xylose, and uronic acids were more digestible in brown midrib genotypes than in normal genotypes. p-Coumaric acid disappearance was higher in heifers consuming normal genotypes than in those on brown midrib mutants. In a second experiment, four Suffolk wethers with ruminal, duodenal, and ileal cannulae were utilized in a 4 x 4 Latin square design. Diets were second-cutting sorghum-sudangrass harvested at prehead stage of maturity as baled hay. Digestibilities were determined in the same manner as for heifers. Brown midrib genotypes had higher hemicellulosic monosaccharides, galactose, and uronic acids than did normal genotypes. Xylose content of the brown midrib mutant of Redlan x Piper was higher than that of the corresponding normal genotype. Total tract galactose digestibility was higher in brown midrib genotypes than in normal genotypes. Total tract hemicellulose digestibility (estimated by summing fractional digestibilities of hemicellulosic monosaccharides) was higher in brown midrib mutants than in normal genotypes.
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PMID:Disappearance of hemicellulosic monosaccharides and alkali-soluble phenolic compounds of normal and brown midrib sorghum x sudangrasses fed to heifers and sheep. 292 37

UDP-glucuronic acid decarboxylase catalyses the reaction responsible for the formation of UDP-xylose and commits assimilate for the biosynthesis of cell wall polysaccharides and glycosylation of proteins. Xylose-rich polymers such as xylans are a feature of dicot secondary walls. Thus a cell culture system of tobacco transformed with the ipt gene from Agrobacterium tumefaciens for cytokinin production and which when manipulated with auxin and sucrose leads to induction of xylogenesis, has been used as a source for purification of the enzyme. UDP-glucuronic acid decarboxylase was purified by ion-exchange, gel filtration and affinity chromatography on Reactive Brown-Agarose. The native enzyme had an apparent M(r) of 220,000 which yielded a single subunit of 87,000 when analysed on SDS-PAGE using silver staining. This appears to be a novel form of the enzyme since a gene family encoding polypeptides around M(r) 40,000 with homology to the fungal enzyme also exists in plants. Using an antibody raised to the native 87 kDa form of the enzyme, this decarboxylase was localised mainly to to cambium and differentiating vascular tissue in tobacco stem, consistent with a role in the provision of UDP-xylose for the synthesis of secondary wall xylan. Further analysis using immunogold electron microscopy localised the 87 kDa UDP-glucuronic acid decarboxylase to the cytosol of developing vascular tissue.
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PMID:Characterisation and immunolocation of an 87 kDa polypeptide associated with UDP-glucuronic acid decarboxylase activity from differentiating tobacco cells (Nicotiana tabacum L.). 1245 69