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PMID: 5704822 Published · ppublish English Journal Article

The availability of carnitine acetyltransferase in mitochondria from guinea-pig liver and other tissues.

The Biochemical journal ·Vol. 110 ·No. 4 ·1968-12-00 ·Pages 739-46

Barker PJ, Fincham NJ, Hardwick DC

Abstract

The carnitine acetyltransferase and glutamate dehydrogenase activities of guinea-pig liver and other tissues were estimated. Both enzymes are wholly mitochondrial, and can only be fully observed after disruption of the mitochondrion. Triton X-100 (0.1%) or freeze-drying revealed more activity than other methods tried. In mitochondria prepared and suspended in 0.25m-sucrose and in cell cytoplasm only small fractions of the total enzymic activity could be observed in guinea-pig liver: on average 7.5% of carnitine acetyltransferase and 5.5% of glutamate dehydrogenase. It is concluded that, in liver or mammary gland of goat, guinea pig or rat, little or no carnitine acetyltransferase is available in vivo to acetyl-CoA outside the mitochondrion.

MeSH Terms
Acyltransferases/metabolism Animals Carnitine/metabolism Coenzyme A/metabolism Cytoplasm Freeze Drying Glutamate Dehydrogenase/metabolism Goats Guinea Pigs In Vitro Techniques Mammary Glands, Animal/enzymology Mitochondria/enzymology Mitochondria, Liver/enzymology Rats Sheep Sucrose Surface-Active Agents
Chemicals
Surface-Active Agents Sucrose Glutamate Dehydrogenase Acyltransferases Carnitine Coenzyme A
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Barker P J
Fincham N J
Hardwick D C
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25 references, click to expand
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
DOI
10.1042/bj1100739
Published
1968-12-00
Pages
739-46
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1187448
Subset
IM
External Links
PubMed source DOI: 10.1042/bj1100739 PMC Full Text View journal details
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