Analysis of myeloperoxidase activity in wound fluids as a marker of infection.

Abstract:

BACKGROUND:Neutrophilic polymorphonuclear leukocytes play a crucial role in the host defence against bacterial and fungal infections. They participate in the inflammatory response through the liberation of peptides and enzymes like myeloperoxidase (MPO). Therefore, MPO has a potential as a marker enzyme for the diagnosis of wound infection. METHODS:Substrate specificities and reaction pathways of MPO were investigated for new MPO substrates: crystal violet, leuco crystal violet, fast blue RR (4-benzoylamino-2,5-dimethoxybenzenediazonium chloride hemi(zinc chloride) salt) and various systematically substituted model substrates based on 2,7-dihydroxy-1-(4-hydroxyphenylazo)naphtalene-3,6-disulphonic acid. In addition, fast blue RR was covalently bound to siloxanes allowing immobilization of the substrate, while cellobiosedehydrogenase was integrated for generation of hydrogen peroxide required by MPO. RESULTS:Elevated concentrations of MPO were found in infected wounds compared with non-infected wounds (92.2 ± 45.0 versus 1.9 ± 1.8 U/mL). Various soluble and immobilized substrates were oxidized by MPO in wound samples and the influence of substrate structure and reaction pathways were elucidated for selected compounds. CONCLUSIONS:Incubation of different MPO substrates with infected wound fluid samples resulted in a clear colour change in the case of elevated MPO concentrations, thus allowing early diagnosis of wound infection.

journal_name

Ann Clin Biochem

authors

Hasmann A,Wehrschuetz-Sigl E,Marold A,Wiesbauer H,Schoeftner R,Gewessler U,Kandelbauer A,Schiffer D,Schneider KP,Binder B,Schintler M,Guebitz GM

doi

10.1258/acb.2011.010249

subject

Has Abstract

pub_date

2013-05-01 00:00:00

pages

245-54

issue

Pt 3

eissn

0004-5632

issn

1758-1001

pii

acb.2011.010249

journal_volume

50

pub_type

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