Linked Life Data

3922278

Source:http://linkedlifedata.com/resource/pubmed/id/3922278

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1985-6-19
pubmed:abstractText
The maltase (EC 3.2.1.20)/glucoamylase (EC 3.2.1.3) complex from rat small intestine brush border, which is able to split alpha (1----4) glucose-sorbitol linkage, was isolated and purified by chromatography on DEAE-Trisacryl M and Sepharose 6B. The complex was homogeneous on polyacrylamide gel electrophoresis. Kinetic parameters were studied on two substrates: maltose and maltitol (Km:1.3 mM and 30 mM, Vmax:200 nmol X min-1 and 15 nmol X min-1, respectively). Inhibition studies were performed with maltose and maltitol as substrates and isomaltitol and delta-gluconolactone as inhibitors. Crossed-inhibition reactions were also performed. The results support the existence of one single catalytic site and this fact was confirmed by physicochemical properties. Similar results were obtained with germ-free rats as well as with conventional rats adapted over 6-12 months to Lycasin 80/55 as the sole source of sugar. Lycasin 80/55, hydrogenated starch hydrolysate, was converted by purified maltase/glucoamylase complex in glucose and sorbitol.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0250-6807
pubmed:author
pubmed:issnType
Print
pubmed:volume
29
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
76-82
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1985
pubmed:articleTitle
New approach to the metabolism of hydrogenated starch hydrolysate: hydrolysis by the maltase/glucoamylase complex of the rat intestinal mucosa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't