| pubmed-article:2717620 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2717620 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:2717620 | lifeskim:mentions | umls-concept:C0074042 | lld:lifeskim |
| pubmed-article:2717620 | pubmed:issue | 9 | lld:pubmed |
| pubmed-article:2717620 | pubmed:dateCreated | 1989-6-9 | lld:pubmed |
| pubmed-article:2717620 | pubmed:abstractText | Saposin A, a heat-stable 16-kDa glycoprotein, was isolated from Gaucher disease spleen and purified to homogeneity. Chemical sequencing from its amino terminus and of peptides obtained by digestion with protease from Staphylococcus aureus strain V-8 demonstrated that saposin A is derived from proteolytic processing of domain 1 of its precursor protein, prosaposin. Processing of prosaposin (70 kDa) also generates three other previously reported saposin proteins, B, C, and D, from its second, third, and fourth domains. Similar to saposin C, saposin A stimulates the hydrolysis of 4-methylumbelliferyl beta-glucoside and glucocerebroside by beta-glucosylceramidase and of galactocerebroside by beta-galactosylceramidase, mainly by increasing the maximal velocity of both reactions. Saposin A is as active as saposin C in these reactions. Saposin A has no significant effect on other sphingolipid and 4-methylumbelliferyl glycoside hydrolases tested. Saposin A has two potential glycosylation sites that appear to be glycosylated. After deglycosylation, saposin A had a subunit molecular mass of 10 kDa and was as active as native saposin A. However, reduction and alkylation abolished the activation. A three-dimensional model comparing saposins A and C reveals significant sequence homology between them, especially preservation of conserved acidic and basic residues in their middle regions. Each appears to possess a conformationally rigid hydrophobic pocket stabilized by three internal disulfide bridges, with amphipathic helical regions interrupted by helix breakers. | lld:pubmed |
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| pubmed-article:2717620 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2717620 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2717620 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2717620 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2717620 | pubmed:month | May | lld:pubmed |
| pubmed-article:2717620 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:O'BrienJ SJS | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:MartinB MBM | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:KishimotoYY | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:YamamotoYY | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:MorimotoSS | lld:pubmed |
| pubmed-article:2717620 | pubmed:author | pubmed-author:KretzK AKA | lld:pubmed |
| pubmed-article:2717620 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2717620 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2717620 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2717620 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2717620 | pubmed:pagination | 3389-93 | lld:pubmed |
| pubmed-article:2717620 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2717620 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2717620 | pubmed:articleTitle | Saposin A: second cerebrosidase activator protein. | lld:pubmed |
| pubmed-article:2717620 | pubmed:affiliation | Department of Neurosciences, University of California, San Diego, School of Medicine, La Jolla 92093. | lld:pubmed |
| pubmed-article:2717620 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2717620 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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