2004
DOI: 10.1042/bj20031416
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Partial amino acid sequence and mRNA analysis of cytosolic pyridoxine-beta-d-glucoside hydrolase from porcine intestinal mucosa: proposed derivation from the lactase-phlorizin hydrolase gene

Abstract: We have previously identified and purified a novel beta-glucosidase, designated PNGH (pyridoxine-5'-beta-D-glucoside hydrolase), from the cytosolic fraction of pig intestinal mucosal. PNGH catalyses the hydrolysis of PNG (pyridoxine-5'-beta-D-glucoside), a plant derivative of vitamin B6 that exhibits partial nutritional bioavailability in humans and animals. Preliminary amino acid sequence analysis indicated regions of close similarity of PNGH to the precursor form of LPH (lactase-phlorizin hydrolase), the bet… Show more

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Cited by 4 publications
(4 citation statements)
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“…LPH, a type of extracellular enzyme that is located in the brush border of the small intestinal epithelium, is the only b-glucosidase in the mammalian intestinal brush border. There are two distinct active sites of LPH for catalytic hydrolysis: one for hydrolyzing lactose and flavonoids, and the other for hydrolyzing phlorizin and b-glucosylceramidase (Tseung et al, 2004). Because LPH is located in the brush border of the small intestinal epithelium (Németh et al, 2003), the flavonoids could be hydrolyzed by LPH once they enter the small intestine.…”
Section: Discussionmentioning
confidence: 99%
“…LPH, a type of extracellular enzyme that is located in the brush border of the small intestinal epithelium, is the only b-glucosidase in the mammalian intestinal brush border. There are two distinct active sites of LPH for catalytic hydrolysis: one for hydrolyzing lactose and flavonoids, and the other for hydrolyzing phlorizin and b-glucosylceramidase (Tseung et al, 2004). Because LPH is located in the brush border of the small intestinal epithelium (Németh et al, 2003), the flavonoids could be hydrolyzed by LPH once they enter the small intestine.…”
Section: Discussionmentioning
confidence: 99%
“…The excised protein band was subjected to trypsin digestion and mass spectrometric analysis (Matrix‐assisted laser desorption ionisation time‐of‐flight tandem mass spectrometry analysis) (Medzihradszky et al ., 2000; Venkataraman et al ., 2005) at the microchemical and proteomics facility at Emory University as described previously (Tseung et al ., 2004; Freeman et al ., 2005). GPS Explorer 2.0 software (Applied Biosystems) and a MASCOT ( http://www.matrixscience.com) search engine were used for identification of peptide fragments.…”
Section: Methodsmentioning
confidence: 99%
“…The proteins were then subjected to trypsin digestion and mass spectrometric analysis (MALDI-TOF-MS/MS analysis) (33) at the microchemical and proteomics facility at Emory University as described previously (34,35). GPS Explorer 2.0 software (Applied Biosystems) and a MASCOT (͗www.matrixscience.com/͘) search engine were used for identification of peptide fragments.…”
Section: Identification Of Cationic Polypeptides Of Vaginal Fluidmentioning
confidence: 99%