Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II.
We purified an antimicrobial protein of 76 residues, denoted bovine antimicrobial protein-1 (BAMP-1), from fetal calf serum using hydrophobic chromatography, gel filtration, and reverse-phase high-performance liquid chromatography. The amino acid sequence of BAMP-1 was similar to that of human apolipoprotein A-II (apo A-II), a major component of high-density lipoprotein (HDL), and the amino acid composition was almost identical to that of a previously reported candidate for bovine apo A-II. BAMP-1 was recovered from the post-HDL fraction, but not from the HDL fraction of the serum and was associated with a small amount of triglycerides (5%, w/w). These results suggest that BAMP-1 is the bovine homologue of apo A-II and is present in almost free form in serum. BAMP-1 showed a weak growth-inhibitory activity against Escherichia coli and yeasts tested in phosphate-buffered saline (PBS).
Motizuki
M
M
Department of Biochemistry 2, Yamanashi Medical University, Nakakoma, Yamanashi 409-3898.
Itoh
T
T
Yamada
M
M
Shimamura
S
S
Tsurugi
K
K
D000595:Amino Acid Sequence; D000818:Animals; D000900:Anti-Bacterial Agents / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D016633:Apolipoprotein A-II / Q000737:chemistry / Q000302:isolation & purification* / Q000494:pharmacology; D002417:Cattle; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000187:drug effects; D006801:Humans; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D000900:Anti-Bacterial Agents; D016633:Apolipoprotein A-II; C112965:bovine antimicrobial protein-1