| pubmed-article:3196299 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C0012984 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C0080103 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C0016787 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C0016788 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C1457869 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C1514468 | lld:lifeskim |
| pubmed-article:3196299 | lifeskim:mentions | umls-concept:C1698986 | lld:lifeskim |
| pubmed-article:3196299 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3196299 | pubmed:dateCreated | 1988-12-28 | lld:pubmed |
| pubmed-article:3196299 | pubmed:abstractText | Canine liver alpha-L-fucosidase was purified to apparent homogeneity by affinity chromatography on agarose-epsilon-aminohexanoyl-fucopyranosylamine. It is composed of multiple forms of a common active subunit of 45-50 kDa, which can aggregate in different combinations to form polymers, predominantly dimers. Antiserum was raised against the purified enzyme. There is negligible residual alpha-L-fucosidase in the tissues of English springer spaniels with the lysosomal storage disease fucosidosis. Although no alpha-L-fucosidase protein was detected by Western blotting or by the purification procedure in the affected tissues, some enzymically inactive cross-reacting material was detected in both normal and affected tissues. This suggests that another protein without alpha-L-fucosidase activity was co-purified with the enzyme. Dog liver alpha-L-fucosidase was precipitated by goat anti-(human liver alpha-L-fucosidase) IgG, indicating homology between the enzymes in the two species. Two purified storage products isolated from the brain of a dog with fucosidosis were used as natural substrates for various preparations of canine liver alpha-L-fucosidase. Analysis of the digestion mixtures by t.l.c. and fast-atom-bombardment mass spectrometry suggests that canine alpha-L-fucosidase acts preferentially on the alpha-(1-3)-linked fucose at the non-reducing end and that removal of alpha-(1-6)-linked asparagine-linked N-acetylglucosamine is rate-limiting in the lysosomal catabolism of fucosylated N-linked glycans. | lld:pubmed |
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| pubmed-article:3196299 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3196299 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3196299 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3196299 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3196299 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:3196299 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3196299 | pubmed:author | pubmed-author:AlhadeffJ AJA | lld:pubmed |
| pubmed-article:3196299 | pubmed:author | pubmed-author:BarkerCC | lld:pubmed |
| pubmed-article:3196299 | pubmed:author | pubmed-author:RogersMM | lld:pubmed |
| pubmed-article:3196299 | pubmed:author | pubmed-author:DellAA | lld:pubmed |
| pubmed-article:3196299 | pubmed:author | pubmed-author:WinchesterBB | lld:pubmed |
| pubmed-article:3196299 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3196299 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3196299 | pubmed:volume | 254 | lld:pubmed |
| pubmed-article:3196299 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3196299 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3196299 | pubmed:pagination | 861-8 | lld:pubmed |
| pubmed-article:3196299 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:3196299 | pubmed:meshHeading | pubmed-meshheading:3196299-... | lld:pubmed |
| pubmed-article:3196299 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3196299 | pubmed:articleTitle | Canine alpha-L-fucosidase in relation to the enzymic defect and storage products in canine fucosidosis. | lld:pubmed |
| pubmed-article:3196299 | pubmed:affiliation | Department of Biochemistry, King's College London, U.K. | lld:pubmed |
| pubmed-article:3196299 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3196299 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3196299 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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