| pubmed-article:35150 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:35150 | lifeskim:mentions | umls-concept:C1524119 | lld:lifeskim |
| pubmed-article:35150 | lifeskim:mentions | umls-concept:C0020289 | lld:lifeskim |
| pubmed-article:35150 | lifeskim:mentions | umls-concept:C0033788 | lld:lifeskim |
| pubmed-article:35150 | lifeskim:mentions | umls-concept:C0020725 | lld:lifeskim |
| pubmed-article:35150 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:35150 | pubmed:dateCreated | 1979-6-11 | lld:pubmed |
| pubmed-article:35150 | pubmed:abstractText | Investigation of the binding characteristics of acid beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase, alpha-D-galactosidase and alpha-L-fucosidase from patients with mucolipidosis II and mucolipidosis III to concanavalin A--Sepharose 4B revealed a 2--10-fold decrease in the proportion of enzyme activities from patients with mucolipidoses II and III that adsorbed on the lectin. Neuraminidase treatment of the unadsorbed enzyme fraction did not significantly increased the proportion of enzyme activities that bound to the concanavalin A--Sepharose 4B. Characterization of acid beta-D-galactosidase from the adsorbed and unadsorbed enzyme fractions of mucolipidosis II and mucolipidosis III patients demonstrated identical apparent Km values of 0.22 mM with respect to 4-methylumbelliferyl beta-D-galactopyranoside, altered pH--activity profiles and heterogeneous isoelectric-focusing patterns. The results of this study support the suggestion of an alteration of a post-translational modification (possibly glycosylation) occurring in mucolipidosis II and mucolipidosis III common to the lysosomal hydrolases that affects the mannoserelated properties of these enzymes. | lld:pubmed |
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| pubmed-article:35150 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:35150 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:35150 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:35150 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:35150 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:35150 | pubmed:author | pubmed-author:MillerA LAL | lld:pubmed |
| pubmed-article:35150 | pubmed:author | pubmed-author:KreigA FAF | lld:pubmed |
| pubmed-article:35150 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:35150 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:35150 | pubmed:volume | 177 | lld:pubmed |
| pubmed-article:35150 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:35150 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:35150 | pubmed:pagination | 409-15 | lld:pubmed |
| pubmed-article:35150 | pubmed:dateRevised | 2010-8-31 | lld:pubmed |
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| pubmed-article:35150 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:35150 | pubmed:articleTitle | Urinary lysosomal hydrolases in mucolipidosis II and mucolipidosis III. | lld:pubmed |
| pubmed-article:35150 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:35150 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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