rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1973-10-10
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pubmed:abstractText |
1. The maximum activities of hexokinase and phosphofructokinase in nervous tissue from 18 different animals from different phyla range from 5.1 to 17.6 and from 24.0mumol/min per g fresh wt. respectively. In any one tissue the activities of these two enzymes are, in general, very similar. The rate of glucose utilization by the brain in vivo is much lower than the activities of hexokinase or phosphofructokinase. It is suggested that the high activities of these enzymes indicate a capacity for glycolysis which may be used by the brain during hypoxia or during conditions of extreme neuronal activity. 2. The activities of 3-oxo acid CoA-transferase and acetoacetyl-CoA thiolase in the nervous tissues range from 1.1 to 15.3 and from 0.7 to 4.5mumol/min per g fresh wt. respectively. Unfortunately the activities of these enzymes cannot be used to estimate maximal flux through the ketone-body-utilization pathway, since they may catalyse reactions that are close to equilibrium. Nonetheless, the presence of these enzymes in nervous tissue from a large variety of animals suggests that the importance of ketone bodies as a fuel for nervous tissue may be widespread in the animal kingdom.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-14114842,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-14402470,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-4227784,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-4321856,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-4342385,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-4588146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-5124783,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-5165621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-5801671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-6048793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/4269208-6061736
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0264-6021
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:volume |
134
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
97-101
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:4269208-Acetoacetates,
pubmed-meshheading:4269208-Acetyl Coenzyme A,
pubmed-meshheading:4269208-Acetyltransferases,
pubmed-meshheading:4269208-Animals,
pubmed-meshheading:4269208-Anura,
pubmed-meshheading:4269208-Birds,
pubmed-meshheading:4269208-Brain,
pubmed-meshheading:4269208-Coenzyme A,
pubmed-meshheading:4269208-Female,
pubmed-meshheading:4269208-Fishes,
pubmed-meshheading:4269208-Hexokinase,
pubmed-meshheading:4269208-Insects,
pubmed-meshheading:4269208-Keto Acids,
pubmed-meshheading:4269208-Lizards,
pubmed-meshheading:4269208-Male,
pubmed-meshheading:4269208-Mice,
pubmed-meshheading:4269208-Nephropidae,
pubmed-meshheading:4269208-Oligochaeta,
pubmed-meshheading:4269208-Phosphofructokinase-1,
pubmed-meshheading:4269208-Rats,
pubmed-meshheading:4269208-Snails,
pubmed-meshheading:4269208-Snakes,
pubmed-meshheading:4269208-Species Specificity,
pubmed-meshheading:4269208-Spinal Cord,
pubmed-meshheading:4269208-Sulfurtransferases,
pubmed-meshheading:4269208-Triturus,
pubmed-meshheading:4269208-Urodela
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pubmed:year |
1973
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pubmed:articleTitle |
Activities of hexokinase, phosphofructokinase, 3-oxo acid coenzyme A-transferase and acetoacetyl-coenzyme A thiolase in nervous tissue from vertebrates and invertebrates.
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pubmed:publicationType |
Journal Article
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