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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1983-4-7
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pubmed:abstractText |
Mucolipidosis III acid hydrolases possess an altered carbohydrate recognition marker needed for their lysosomal localization. As a result of this alteration, a portion of these enzymes is secreted from the cell to the extracellular spaces. The structural changes that may have occurred to one of these secreted enzymes, beta-N-acetyl-d-hexosaminidase A (EC 3.2.1.52) were investigated. Normal and mucolipidosis III urinary beta-N-acetyl-d-hexosaminidase A were purified to apparent homogeneity by using affinity [Sepharose-2-acetamido-N-(epsilon-aminocaproyl)-2-deoxy-beta- d-glucopyranosylamine] and ion-exchange (DEAE- and CM-cellulose) chromatography. Sodium dodecyl sulphate/polyacrylamide-slab-gel electrophoresis showed that both enzymes had similar subunit patterns consisting of apparent mol.wts. of 68000, 60000-58000, 55000 and 29000. Differences, however, were noted in the relative proportions of the protein bands where the normal urinary beta-N-acetyl-d-hexosaminidase A contained predominantly the smaller subunits, whereas the mucolipidosis III enzyme had a predominance of the larger subunits. The binding of mucolipidosis III beta-N-acetyl-d-hexosaminidase A to Ricinus communis lectin and concanavalin A with and without endo-beta-N-acetyl-d-glucosaminidase H treatment indicated that the mutation leads to a modification of a portion of the normally occurring high-mannose-type oligosaccharide units to the complex-type. This was further supported by carbohydrate compositional analysis, which revealed a mannose/galactose ratio of 2.1 for the mucolipidosis III beta-N-acetyl-d-hexosaminidase A compared with a ratio of 3.5 for the normal enzyme. Our results indicate that as a result of their inability to be properly localized to the lysosome the majority of the mucolipidosis III lysosomal hydrolase high-mannose oligosaccharide units are further processed to the complex-type before secretion of predominantly higher-molecular-weight subunits from the cell.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-152578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-242317,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-36886,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-428391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-4326772,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-4345092,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-4346288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-435265,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-4359899,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-4362060,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6251056,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6262380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6452876,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6455422,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6459926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6460470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6938953,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6989821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-6989822,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7115350,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7236240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7356669,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7378875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7391040,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-7396846,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-822246,
http://linkedlifedata.com/resource/pubmed/commentcorrection/6219664-892710
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
207
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
421-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:6219664-Carbohydrates,
pubmed-meshheading:6219664-Chromatography, Ion Exchange,
pubmed-meshheading:6219664-Concanavalin A,
pubmed-meshheading:6219664-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:6219664-Female,
pubmed-meshheading:6219664-Hexosaminidases,
pubmed-meshheading:6219664-Humans,
pubmed-meshheading:6219664-Lectins,
pubmed-meshheading:6219664-Male,
pubmed-meshheading:6219664-Mucolipidoses,
pubmed-meshheading:6219664-beta-N-Acetylhexosaminidases
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pubmed:year |
1982
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pubmed:articleTitle |
Mucolipidosis III beta-N-acetyl-D-hexosaminidase A. Purification and properties.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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