Linked Life Data

2450702

Source:http://linkedlifedata.com/resource/pubmed/id/2450702

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-5-5
pubmed:abstractText
In this paper we studied the properties of 3-hydroxy-3-methylglutaryl-CoA lyase (HMG-CoA lyase) in human skin fibroblasts. The enzyme was found to exhibit an absolute requirement for divalent cations such as magnesium. Furthermore, dithiothreitol was necessary for full activity. The enzyme was found to be maximally active at pH 9.25. When measured at this pH in the presence of magnesium and dithiothreitol enzyme activity was high enough to be determined by simple spectrophotometry by measuring the amounts of acetoacetate produced. The results obtained suggest that the large variation in the values reported in literature for the activity of HMG-CoA lyase in human skin fibroblasts is due to the fact that the enzyme shows little activity at pH values below 8.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0009-8981
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
171
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-101
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
3-Hydroxy-3-methylglutaryl-CoA lyase in human skin fibroblasts: study of its properties and deficient activity in 3-hydroxy-3-methylglutaric aciduria patients using a simple spectrophotometric method.
pubmed:affiliation
Department of Pediatrics, University Hospital Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article