| pubmed-article:10744681 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C0005220 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1708096 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1709634 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10744681 | lifeskim:mentions | umls-concept:C1707271 | lld:lifeskim |
| pubmed-article:10744681 | pubmed:issue | 14 | lld:pubmed |
| pubmed-article:10744681 | pubmed:dateCreated | 2000-5-8 | lld:pubmed |
| pubmed-article:10744681 | pubmed:abstractText | Lysosomal beta-D-galactosidase (beta-gal), the enzyme deficient in the autosomal recessive disorders G(M1) gangliosidosis and Morquio B, is synthesized as an 85-kDa precursor that is C-terminally processed into a 64-66-kDa mature form. The released approximately 20-kDa proteolytic fragment was thought to be degraded. We now present evidence that it remains associated to the 64-kDa chain after partial proteolysis of the precursor. This polypeptide was found to copurify with beta-gal and protective protein/cathepsin A from mouse liver and Madin-Darby bovine kidney cells and was immunoprecipitated from human fibroblasts but not from fibroblasts of a G(M1) gangliosidosis and a galactosialidosis patient. Uptake of wild-type protective protein/cathepsin A by galactosialidosis fibroblasts resulted in a significant increase of mature and active beta-gal and its C-terminal fragment. Expression in COS-1 cells of mutant cDNAs encoding either the N-terminal or the C-terminal domain of beta-gal resulted in the synthesis of correctly sized polypeptides without catalytic activity. Only when co-expressed, the two subunits associate and become catalytically active. Our results suggest that the C terminus of beta-gal is an essential domain of the catalytically active enzyme and provide evidence that lysosomal beta-galactosidase is a two-subunit molecule. These data may give new significance to mutations in G(M1) gangliosidosis patients found in the C-terminal part of the molecule. | lld:pubmed |
| pubmed-article:10744681 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10744681 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10744681 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10744681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10744681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10744681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10744681 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10744681 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10744681 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10744681 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10744681 | pubmed:author | pubmed-author:d'AzzoAA | lld:pubmed |
| pubmed-article:10744681 | pubmed:author | pubmed-author:BontenEE | lld:pubmed |
| pubmed-article:10744681 | pubmed:author | pubmed-author:van der... | lld:pubmed |
| pubmed-article:10744681 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10744681 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:10744681 | pubmed:volume | 275 | lld:pubmed |
| pubmed-article:10744681 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10744681 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10744681 | pubmed:pagination | 10035-40 | lld:pubmed |
| pubmed-article:10744681 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10744681 | pubmed:meshHeading | pubmed-meshheading:10744681... | lld:pubmed |
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| pubmed-article:10744681 | pubmed:meshHeading | pubmed-meshheading:10744681... | lld:pubmed |
| pubmed-article:10744681 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10744681 | pubmed:articleTitle | Processing of lysosomal beta-galactosidase. The C-terminal precursor fragment is an essential domain of the mature enzyme. | lld:pubmed |
| pubmed-article:10744681 | pubmed:affiliation | Department of Genetics, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA. | lld:pubmed |
| pubmed-article:10744681 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10744681 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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