Purification, Primary Structure, and Antimicrobial Activities of Bovine Apolipoprotein A-II.
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概要
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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-Il 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).
- 社団法人 日本生化学会の論文
著者
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Shimamura Seiichi
Biochemical Research Laboratory Morinaga Milk Industry Co. Ltd.
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ITOH Takehito
Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd.
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Yamada Muneo
Biochemical Research Laboratory Morinaga Milk Industry
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Motizuki Mitsuyoshi
Department Of Biochemistry 2 Faculty Of Medicine University Of Yamanashi
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Tsurugi Kunio
Department Of Biochemistry 2 Faculty Of Medicine University Of Yamanashi
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YAMADA Muneo
Biochemical Research Laboratory, Morinaga Milk Industry Co., Ltd.
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