caa a22 4500 477120393 CHVBK 20180405111635.0 cr unu---uuuuu 170330e19961201xx s 000 0 eng 10.1007/BF00229470 doi (NATIONALLICENCE)springer-10.1007/BF00229470 Purification of carnitine acetyltransferase from skeletal muscle of the camel ( Camelus dromedarius ) [Elektronische Daten] [A. Alhomida, A. Duhaiman, A. Al-Jafari, M. Junaid] 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 β-oxidation of fatty acids. Purification and characterization of CAT from desert animal species may help in explaining the involvement of secondary pathways for energy production in these species. In this paper, we report the purification 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 DEAF-Sepharose, agarose-Co A and Superose 12 gel filtration columns. CAT was purified by 2937-fold to a specific activity of 94 Units mg−1. The purified CAT was a monomer of 59 kDa as judged by native and SDS-PAGE, and showed a pl of 5.2. The enzyme displayed maximum activity with propionyl-Co A. Apparent Km for acetyl-, propionyl- and butyryl-Co A were 27.7, 17.3 and 29 μM respectively, while palmitoyl-Co A was not a substrate. Kluwer Academic Publishers, 1996 carnitine acetyltransferase nationallicence camel nationallicence skeletal muscle nationallicence β-oxidation nationallicence Alhomida A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut Duhaiman A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut Al-Jafari A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut Junaid M. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/2(1996-12-01), 95-101 0300-8177 165:2<95 1996 165 11010 https://doi.org/10.1007/BF00229470 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/BF00229470 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Alhomida A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut NATIONALLICENCE 700 1- Duhaiman A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut NATIONALLICENCE 700 1- Al-Jafari A. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut NATIONALLICENCE 700 1- Junaid M. Department of Biochemistry, College of Science, King Saud University, P.O. Box 2455, 11451, Riyadh, Saudi Arabia aut NATIONALLICENCE 773 0- Molecular and Cellular Biochemistry Kluwer Academic Publishers; http://www.wkap.nl 165/2(1996-12-01), 95-101 0300-8177 165:2<95 1996 165 11010 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer