| pubmed-article:291966 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0031945 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0005516 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0017776 | lld:lifeskim |
| pubmed-article:291966 | lifeskim:mentions | umls-concept:C0024742 | lld:lifeskim |
| pubmed-article:291966 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:291966 | pubmed:dateCreated | 1980-1-24 | lld:pubmed |
| pubmed-article:291966 | pubmed:abstractText | Human beta-glucuronidase (beta-D-glucuronide glucuronosohydrolase, EC 3.2.1.31), like many other glycoprotein lysosomal hydrolases, is subject to receptor-mediated endocytosis by fibroblasts. Prior work demonstrated charge heterogeneity in beta-glucuronidase and showed that high-uptake forms are more acidic than slowly internalized forms. Considerable indirect evidence implicated mannose 6-phosphate as an essential part of the recognition marker on high-uptake enzyme forms. Here we report the purification of beta-glucuronidase from human spleen and demonstrate enzymatically that mannose 6-phosphate is released on acid hydrolysis of pure enzyme varies directly with its susceptibility to pinocytosis by fibroblasts. Enzyme forms resolved by CM-Sephadex chromatography differed over an 18-fold range in uptake rate and in mannose 6-phosphate content. The most acidic forms had 4.4 mol of mannose 6-phosphate per mol of enzyme. The mannose 6-phosphate was released from the enzyme by treatment with endoglycosidase H with concomitant loss of susceptibility to adsorptive endocytosis. Thus, these studies provide direct evidence that mannose 6-phosphate is present on high-uptake enzyme forms, that it is present in the recognition marker for uptake, and that it is present on oligosaccharide that is released by endoglycosidase H. | lld:pubmed |
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| pubmed-article:291966 | pubmed:language | eng | lld:pubmed |
| pubmed-article:291966 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:291966 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:291966 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:291966 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:291966 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:291966 | pubmed:author | pubmed-author:LowryO HOH | lld:pubmed |
| pubmed-article:291966 | pubmed:author | pubmed-author:SlyW SWS | lld:pubmed |
| pubmed-article:291966 | pubmed:author | pubmed-author:SAZH JHJ | lld:pubmed |
| pubmed-article:291966 | pubmed:author | pubmed-author:NatowiczM RMR | lld:pubmed |
| pubmed-article:291966 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:291966 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:291966 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:291966 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:291966 | pubmed:pagination | 4322-6 | lld:pubmed |
| pubmed-article:291966 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:291966 | pubmed:year | 1979 | lld:pubmed |
| pubmed-article:291966 | pubmed:articleTitle | Enzymatic identification of mannose 6-phosphate on the recognition marker for receptor-mediated pinocytosis of beta-glucuronidase by human fibroblasts. | lld:pubmed |
| pubmed-article:291966 | pubmed:publicationType | Journal Article | lld:pubmed |
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