Purification and characterization of variants of acyl-CoA-binding protein in the bovine liver.
Four differently modified forms of acyl-CoA-binding protein (ACBP) were identified in ACBP purified from bovine liver. The majority of the purified ACBP was focused at pH 5.9 in isoelectric focusing and could be shown to be N-acetylated ACBP without any further modifications. Two minor peaks were focused at pH 5.25 and 4.85 respectively. Mass spectrometry and sequence determination showed that the pI 5.25 form was acetylated at Lys18 and that the pI 4.85 form was malonylated in the same position. Furthermore, it could be shown that non-enzymic glycosylation occurred during purification. The acetylated and malonylated variants of ACBP were only found in adult cattle.
Jensen
M S
MS
Institute of Biochemistry, Odense University, Denmark.
Højrup
P
P
Rasmussen
J T
JT
Knudsen
J
J
D000595:Amino Acid Sequence; D000818:Animals; D002352:Carrier Proteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D002417:Cattle; D026261:Diazepam Binding Inhibitor; D005227:Fatty Acids / Q000378:metabolism; D014644:Genetic Variation; D007525:Isoelectric Focusing; D008099:Liver / Q000378:metabolism*; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010449:Peptide Mapping
D002352:Carrier Proteins; D026261:Diazepam Binding Inhibitor; D005227:Fatty Acids