Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1983-4-15
pubmed:abstractText
The proportion of active (unphosphorylated) branched chain alpha-ketoacid dehydrogenase was determined in tissues from rats in different metabolic states. Hearts from normal, high-protein, and low-protein fed rats contained about 45% of the enzyme in the active form. Only 10-20% of the enzyme was active in hearts of fasted and diabetic rats. Virtually all of the liver enzyme was in the active form in fed, fasted, diabetic and high-protein fed animals. Protein starved rats, however, exhibited a dramatic decrease in both the % active form and total amount of liver enzyme. Kidneys from normal, fasted, diabetic and high-protein fed rats contained 70-80% of the enzyme in the active form. The % active form of the kidney enzyme decreased in protein starved rats, but less dramatically than in liver. Covalent modification is concluded to be important for in vivo regulation of the branched chain alpha-ketoacid dehydrogenase complex.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
111
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
74-81
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
Activity state of the branched chain alpha-ketoacid dehydrogenase complex in heart, liver, and kidney of normal, fasted, diabetic, and protein-starved rats.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't