Linked Life Data

15632

Source:http://linkedlifedata.com/resource/pubmed/id/15632

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1977-6-30
pubmed:abstractText
The catalytic properties of a neutral alpha-glucosidase purified to homogeneity from human renal cortex are described. The pH optimum was 6 (maltose and starch). It has a broad range of substrate specificity, hydrolysing di- and oligosaccharides with alpha (1 leads to 2), alpha (1 leads to 3), alpha (1 leads to 4) and alpha (1 leads to 6) linkages. Glucosidase action on maltosaccharides was associated with pronounced substrate inhibition at concentrations exceeding 0,5 mM. It also hydrolyses polysaccharides as starch and glycogen. The Km and Vmax values for the various substrates were determined. The enzymes exhibited intrinsic transglucosylase activity. It catalysed glucosyl-transfer reaction from maltose to itself (disproportionation). Mixed substrate inhibition studies, inhibition studies and heat inactivation are interpreted in terms of the existence of at least two interacting sites on the enzyme.
pubmed:language
fre
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-9084
pubmed:author
pubmed:issnType
Print
pubmed:volume
59
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-14
pubmed:dateRevised
2009-10-27
pubmed:meshHeading
pubmed:year
1977
pubmed:articleTitle
[Catalytic properties of a neutral alpha-glucosidase from human kidney].
pubmed:publicationType
Journal Article, English Abstract