Linked Life Data

3144105

Source:http://linkedlifedata.com/resource/pubmed/id/3144105

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1989-1-26
pubmed:abstractText
The glycolytic and aerobic oxidative capacity in skeletal muscle was investigated to reveal if the decrease seen in muscle protein synthesis is accompanied by a fall in the enzymatic capacity to oxidize substrates. Six patients undergoing elective abdominal surgery were investigated by percutaneous muscle biopsies taken before surgery and on the first and third postoperative days. Protein synthesis as assessed by the polyribosome concentration was 40% lower on the third day postoperatively than before surgery (p less than 0.01). The glycolytic and oxidative capacity was evaluated by determining the activity of eight key enzymes in the intracellular oxidative metabolism, namely total creatine kinase (CK), the isozymes CK-MB and mitochondrial CK, lactate dehydrogenase, citrate synthase, aspartate aminotransferase, and phosphofructokinase, and also the concentration of myoglobin. None of these parameters were affected in the immediate postoperative period independently of the provision of nutritional support. It was concluded that the decrease in protein synthesis is not accompanied by a concomitant decline in the enzymatic oxidative capacity in skeletal muscle in the period immediately following elective surgery.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0001-5482
pubmed:author
pubmed:issnType
Print
pubmed:volume
154
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-94
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Enzymatic capacity and protein synthesis in human muscle postoperatively.
pubmed:affiliation
Department of Anesthesiology and Intensive Care, Huddinge University Hospital, Stockholm, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't