Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II.

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 Biochem

journal_title

Journal of biochemistry

authors

Motizuki M,Itoh T,Yamada M,Shimamura S,Tsurugi K

doi

10.1093/oxfordjournals.jbchem.a021990

subject

Has Abstract

pub_date

1998-04-01 00:00:00

pages

675-9

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

123

pub_type

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