Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
1
|
| pubmed:dateCreated |
1990-9-20
|
| pubmed:abstractText |
Enzymatic transglucosylation from maltose to L-ascorbic acid (AA) with mammalian tissue homogenates was determined by a high-performance liquid chromatography method and compared with the reaction catalyzed by alpha-glucosidase from Aspergillus niger. The homogenates of small intestine and kidney had a high transglucosylase activity to form a new type of glucosylated AA, which was associated with alpha-glucosidase activity. The new compound was demonstrated to be an equimolar conjugate of AA and glucose by the spectral and quantitative analyses. In particular, it showed a high stability in a neutral solution and no reducing activity toward cytochrome c and a dye. These properties were very different from those of AA and L-ascorbic acid alpha-glucoside formed with alpha-glucosidase from A. niger, but they were consistent with those of L-ascorbic acid 2-O-phosphate and L-ascorbic acid 2-O-sulfate. Moreover, it exhibited a reducing power associated with AA after mild acid hydrolysis or treatment with rat intestinal alpha-glucosidase. These results indicate that it should be assigned the 2-O-alpha-glucoside structure. Consequently, it is concluded that mammalian alpha-glucosidase is able to form a very stable and nonreducing form of glucosylated AA through a specific transglucosylation reaction distinct from that of microbial alpha-glucosidase.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Ascorbic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Glucose,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrochloric Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Maltose,
http://linkedlifedata.com/resource/pubmed/chemical/alpha-Glucosidases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0006-3002
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
20
|
| pubmed:volume |
1035
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
44-50
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:2200520-Animals,
pubmed-meshheading:2200520-Ascorbic Acid,
pubmed-meshheading:2200520-Aspergillus niger,
pubmed-meshheading:2200520-Chromatography, High Pressure Liquid,
pubmed-meshheading:2200520-Enzyme Stability,
pubmed-meshheading:2200520-Glucose,
pubmed-meshheading:2200520-Guinea Pigs,
pubmed-meshheading:2200520-Hydrochloric Acid,
pubmed-meshheading:2200520-Hydrolysis,
pubmed-meshheading:2200520-Intestine, Small,
pubmed-meshheading:2200520-Kidney,
pubmed-meshheading:2200520-Male,
pubmed-meshheading:2200520-Maltose,
pubmed-meshheading:2200520-Organ Specificity,
pubmed-meshheading:2200520-Oxidation-Reduction,
pubmed-meshheading:2200520-Rats,
pubmed-meshheading:2200520-Rats, Inbred Strains,
pubmed-meshheading:2200520-Spectrophotometry, Ultraviolet,
pubmed-meshheading:2200520-alpha-Glucosidases
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Formation of a stable L-ascorbic acid alpha-glucoside by mammalian alpha-glucosidase-catalyzed transglucosylation.
|
| pubmed:affiliation |
Department of Immunochemistry, Faculty of Pharmaceutical Sciences, Okayama University, Japan.
|
| pubmed:publicationType |
Journal Article
|