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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1988-11-22
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pubmed:abstractText |
Gaucher spleen sphingolipid activator protein 2 was fractionated into concanavalin A binding- and non-binding fractions. These fractions each contained several bands on non-denaturing polyacrylamide gel electrophoresis (PAGE). The two fractions were further fractionated by electroblotting the proteins from preparative gels onto nitrocellulose, staining with Ponceau S to locate the bands of protein and then eluting the protein components from the nitrocellulose. A total of ten fractions, each containing only one or two major components, was collected. All of these subfractions activated beta-glucocerebrosidase and sphingomyelinase and most subfractions also activated beta-galactocerebrosidase. The structural relationship of the bands was investigated using endoglycosidase digestions. The results indicated that the two bands with the fastest mobility on non-denaturing PAGE did not contain any carbohydrate. The remaining bands showed only limited or partial digestion with endoglycosidase H and endoglycosidase D, but were readily hydrolysed with endoglycosidase F. The products of these digestions included bands with similar mobilities to the non-carbohydrate containing bands.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-1140409,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-1148261,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-13071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-2429581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-2444214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3019390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3024666,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3099116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3111543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3518703,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3661996,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3771578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3800908,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3830174,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3921288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3933429,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-3966805,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-4005041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-4027262,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-4037311,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-5075513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-5288260,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6096798,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6256275,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6266278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6268176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6274912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6303435,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6615847,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6712963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-6789775,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-7126630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/3178760-942051
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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 |
Aug
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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 |
15
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pubmed:volume |
254
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
77-84
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:3178760-Concanavalin A,
pubmed-meshheading:3178760-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3178760-Galactosylceramidase,
pubmed-meshheading:3178760-Gaucher Disease,
pubmed-meshheading:3178760-Glucosylceramidase,
pubmed-meshheading:3178760-Glycoproteins,
pubmed-meshheading:3178760-Glycoside Hydrolases,
pubmed-meshheading:3178760-Humans,
pubmed-meshheading:3178760-Saposins,
pubmed-meshheading:3178760-Sphingolipid Activator Proteins,
pubmed-meshheading:3178760-Sphingomyelin Phosphodiesterase,
pubmed-meshheading:3178760-Spleen
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pubmed:year |
1988
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pubmed:articleTitle |
Analysis of the multiple forms of Gaucher spleen sphingolipid activator protein 2.
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pubmed:affiliation |
Department of Chemical Pathology, Adelaide Children's Hospital Incorp., South Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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