Abstract
Comparatively large amounts of an acyl-CoA dehydrogenase have been obtained from pig kidney by a procedure which does not involve prior isolation of mito- chondria. The pattern of substrate specificity and the extent of substrate-induced bleaching of the flavin chromophore, using butyryl-, octanoyl-, and palmitoyl-CoA, suggest that the enzyme be classified as a general acyl-CoA dehydrogenase. The purified flavoprotein exhibits absorbance ratios at 272, 373, and 446 nm of 5.7:0.65:1.0, respectively, with an ex- tinction coefficient for bound flavin adenine dinucleotide (FAD) of 15.4 mM-' cm-' at 446 nm. Gel filtration, NaDodSO, gel electrophoresis, and amino acid analysis in- dicate that the enzyme is a tetramer, comprised of subunits of about 42 000 molecular weight, containing 3-4 molecules Mammalian fatty acyl-CoA dehydrogenases are flavo- proteins participating in the first dehydrogenation step of fatty acid @-oxidation which leads to the formation of a,@-unsat- urated acyl-CoA derivatives (Beinert, 1963). The reducing equivalents are then passed to a second component, electron transfer flavoprotein (ETF;' Crane et al., 1956), which in- teracts with the respiratory chain, possibly at the level of a
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
