rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
3
|
pubmed:dateCreated |
1987-2-24
|
pubmed:abstractText |
The anomeric form of glucose produced by glucose-6-phosphatase was studied using an apparatus that specifically measures beta-D-glucose. The time course of beta-D-glucose formation from glucose-6-P by glucose-6-phosphatase is essentially linear. In the presence of mutarotase, this rate is reduced to 70% of that obtained in the absence of mutarotase. When detergent treated microsomes were used, the rate of beta-D-glucose formation is unaffected by mutarotase. These results suggest that only beta-anomer of glucose is produced by microsomal glucose-6-phosphatase and this specificity is determined by translocase for glucose-6-P or glucose. It was also demonstrated that alpha-D-glucose is the substrate for glucokinase.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0006-291X
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
141
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
931-6
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:3028393-Animals,
pubmed-meshheading:3028393-Carbohydrate Epimerases,
pubmed-meshheading:3028393-Glucokinase,
pubmed-meshheading:3028393-Glucose,
pubmed-meshheading:3028393-Glucose-6-Phosphatase,
pubmed-meshheading:3028393-Glucose-6-Phosphate,
pubmed-meshheading:3028393-Glucosephosphates,
pubmed-meshheading:3028393-Kinetics,
pubmed-meshheading:3028393-Microsomes, Liver,
pubmed-meshheading:3028393-Octoxynol,
pubmed-meshheading:3028393-Polyethylene Glycols,
pubmed-meshheading:3028393-Rats,
pubmed-meshheading:3028393-Stereoisomerism,
pubmed-meshheading:3028393-Substrate Specificity
|
pubmed:year |
1986
|
pubmed:articleTitle |
Anomer specificity of glucose-6-phosphatase and glucokinase.
|
pubmed:publicationType |
Journal Article,
Comparative Study
|