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J. Biol. Chem., Vol. 262, Issue 31, 14891-14894, Nov, 1987
CE Ooi, J Weiss, P Elsbach, B Frangione and B Mannion
We have isolated, after limited proteolysis of the
bactericidal/permeability-increasing protein (BPI) of human neutrophils, a
25-kDa fragment that possesses the bactericidal and envelope-altering
activities of the 60-kDa parent protein. On a molar basis, the fragment is
as potent as holo-human BPI against rough Escherichia coli, is more potent
than holo-BPI against more resistant smooth E. coli, and retains the
specificity of BPI toward Gram-negative bacteria. NH2-terminal amino acid
sequence analysis shows that the fragment is derived from the NH2 terminus
of the BPI molecule. These findings suggest that all of the molecular
determinants of the antibacterial properties of BPI reside within the
NH2-terminal 25-kDa segment, implying a novel structural/functional
organization for a cytotoxic protein.
A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein
Department of Medicine, New York University School of Medicine, New York 10016.
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