Abstract:
: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).
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Motizuki M,Itoh T,Yamada M,Shimamura S,Tsurugi Kdoi
10.1093/oxfordjournals.jbchem.a021990subject
Has Abstractpub_date
1998-04-01 00:00:00pages
675-9issue
4eissn
0021-924Xissn
1756-2651journal_volume
123pub_type
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