As. Alhomida et al., PURIFICATION OF CARNITINE ACETYLTRANSFERASE FROM SKELETAL-MUSCLE OF THE CAMEL (CAMELUS-DROMEDARIUS), Molecular and cellular biochemistry, 165(2), 1996, pp. 95-101
The enzyme carnitine acetyltransferase (CAT) catalyzes the reversible
transfer of short-chain acyl groups between coenzyme A and L-carnitine
, and hence, plays an important role in the beta-oxidation of fatty ac
ids. Purification and characterization of CAT from desert animal speci
es may help in explaining the involvement of secondary pathways for en
ergy production in these species. In this paper, we report the purific
ation and partial characterization of CAT from the Arabian camel. CAT
was purified from the skeletal muscle of the Arabian camel by ammonium
sulfate and acetone fractionation, followed by chromatography on DEAE
-Sepharose, agarose-Co A and Superose 12 gel filtration columns. CAT w
as purified by 2937-fold to a specific activity of 94 Units mg(-1). Th
e purified CAT was a monomer of 59 kDa as judged by native and SDS-PAG
E, and showed a pi of 5.2. The enzyme displayed maximum activity with
propionyl-Co A. Apparent K-m for acetyl-, propionyl- and butyryl-Co A
were 27.7, 17.3 and 29 mu M respectively, while palmitoyl-Co A was not
a substrate.