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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1981-9-15
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pubmed:abstractText |
We have previously defined two isozymes of neutral alpha-glucosidase (alpha-D-glucoside glucohydrolase, EC 3.2.1.20) on the basis of differences in electrophoretic mobility and designated these neutral alpha-glucosidase AB and alpha-glucosidase C (Swallow, D.M., Corney, G., Harris, H. and Hirschhorn, R. (1975) Ann. Hum. Gen. 38, 391-406). We now describe differences between the two isozymes with respect to molecular weight, solubility in (NH4)2SO4, glycosylation, isoelectric point and substrate specificities. Neutral alpha-glucosidase C is precipitable in 40-60% (NH4)2SO4, has a molecular weight of 92 000, an isoelectric point of 5.5 and releases glucose from glycogen as well as from low molecular weight artificial and natural substrates containing alpha 1-4 glucosidic linkages. Neutral alpha-glucosidase AB precipitates at 0-40% (NH4)2SO4, binds to concanavalin A, has a molecular weight of greater than 150 000, and does not utilize alpha 1-4 linked glucose substrates larger than a disaccharide. Neutral alpha-glucosidase AB migrates more rapidly to the anode than alpha-glucosidase C when agarose, Cellogel, acrylamide or starch are used as support media. Both isozymes are equally inhibited by Zn2+.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cations, Divalent,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosidases,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose,
http://linkedlifedata.com/resource/pubmed/chemical/Trisaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:volume |
658
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
248-61
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:7018580-Cations, Divalent,
pubmed-meshheading:7018580-Electrophoresis,
pubmed-meshheading:7018580-Female,
pubmed-meshheading:7018580-Glucosidases,
pubmed-meshheading:7018580-Glycogen,
pubmed-meshheading:7018580-Humans,
pubmed-meshheading:7018580-Isoelectric Point,
pubmed-meshheading:7018580-Isoenzymes,
pubmed-meshheading:7018580-Maltose,
pubmed-meshheading:7018580-Molecular Weight,
pubmed-meshheading:7018580-Pregnancy,
pubmed-meshheading:7018580-Substrate Specificity,
pubmed-meshheading:7018580-Trisaccharides,
pubmed-meshheading:7018580-alpha-Glucosidases
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pubmed:year |
1981
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pubmed:articleTitle |
Characterization of neutral isozymes of human alpha-glucosidase: differences in substrate specificity, molecular weight and electrophoretic mobility.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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