Purification of the medium-chain/long-chain (COT/CPT) carnitine acyltransferase of rat liver microsomes.

Abstract:

:A procedure for the purification of the rat liver microsomal carnitine octanoyltransferase (COT) that catalyzes the reversible formation of medium-chain and long-chain acylcarnitines from acyl-coenzyme A is described. The K0.5 for L-carnitine is 0.6 mM and the K0.5 for both decanoyl-CoA and palmitoyl-CoA is 0.6 microM. The Vmax with decanoyl-CoA is approximately fourfold greater than the Vmax with palmitoyl-CoA. The enzyme is monomeric, sodium dodecyl sulfate-polyacrylamide gel electrophoresis gives a molecular weight of 50,100, and molecular sieving gives a molecular weight of 54,300. Purified COT does not cross-react with either antimitochondrial carnitine palmitoyltransferase or antiperoxisomal COT antibodies. It also does not form a covalent adduct when incubated with etomoxiryl-CoA. Microsomal COT is a different protein than either mitochondrial carnitine palmitoyltransferase or peroxisomal COT.

journal_name

Protein Expr Purif

authors

Murthy MS,Bieber LL

doi

10.1016/1046-5928(92)90059-6

keywords:

subject

Has Abstract

pub_date

1992-02-01 00:00:00

pages

75-9

issue

1

eissn

1046-5928

issn

1096-0279

pii

1046-5928(92)90059-6

journal_volume

3

pub_type

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