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• W2049309723 abstract "Abstract Aim: Cervico‐vaginal fluid (CVF) may provide insight into the biochemical pathways of human reproduction and parturition. The aim of this study was to establish a 2‐D electrophoretic map of human CVF in healthy, pregnant women at term. Methods: CVF was collected, concentrated and processed by routine 2‐D polyacrylamide gel electrophoresis using pH 4–7‐immobilised pH gradient strips and 8–16% gradient polyacrylamide gels. Imaged gels were analysed, yielding more than 400 proteins. A total of 157 proteins were common to all gels with a subgroup of the most abundant proteins being excised and characterised either by MALDI or by electrospray ion‐trap mass spectrometry. Results: Twenty‐one proteins were successfully identified, yielding 15 different proteins. These included blood transport proteins (albumin and transthyretin); a structural protein (β‐actin); proteins involved in fatty acid metabolism (fatty acid‐binding protein and acetyl‐CoA‐binding protein); a calcium‐binding protein (annexin III); an anti‐inflammatory cytokine (interleukin‐1 receptor antagonist); proteinase inhibitors (α‐1‐antitrypsin, monocyte/neutrophil elastase inhibitor, squamous cell carcinoma antigen‐1 and cystatin A); and enzymes involved in oxidative stress defence (thioredoxin, peroxiredoxin 2, glutathione S‐transferase P and copper,zinc superoxide dismutase). Conclusion: CVF is a complex body fluid consisting of both endogenous and environmental proteins. The putative role of some of these proteins in the human reproductive tract is discussed." @default.
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• W2049309723 date "2007-01-29" @default.
• W2049309723 modified "2023-10-13" @default.
• W2049309723 title "Proteomic analysis and characterisation of human cervico-vaginal fluid proteins" @default.
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• W2049309723 doi "https://doi.org/10.1111/j.1479-828x.2006.00671.x" @default.
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