Optical characterization of armadillo acyl-CoA binding protein.
Acyl-CoA binding protein (ACBP) and fatty acid binding protein (FABP) are intracellular transporters of activated and free fatty acids, respectively. Unlike other tissues with active lipid metabolism, armadillo Harderian gland contains much more ACBP than FABP. To characterize armadillo ACBP structure and binding properties, we produced it in Escherichia coli and carried out detailed fluorescence and circular dichroism spectroscopy studies. The K(D) for palmitoyl-CoA, measured directly by fluorescence and rotatory power, was 34+/-12 and 75+/-39 nM, respectively. The structure of armadillo ACBP appears to be very similar to that of bovine and rat liver ACBPs.
Cavagnari
Brian M
BM
Facultad de Farmacia y Bioquímica (UBA-CONICET), Instituto de Química y Fisicoquímica Biológicas, Juni;n 956, 1113, Buenos Aires, Argentina.
Milikowski
Daniel
D
Haller
Jorge F
JF
Zanek
María C
MC
Santomé
José A
JA
Ermácora
Mario R
MR
D000595:Amino Acid Sequence; D000818:Animals; D001135:Armadillos; D001483:Base Sequence; D002417:Cattle; D002942:Circular Dichroism; D026261:Diazepam Binding Inhibitor / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D011485:Protein Binding; D011506:Proteins / Q000737:chemistry; D051381:Rats; D013050:Spectrometry, Fluorescence; D013696:Temperature; D013816:Thermodynamics; D014466:Ultraviolet Rays
D026261:Diazepam Binding Inhibitor; D011506:Proteins