Activity of selected glycosidases and availability of their substrates in bovine placenta during pregnancy and parturition with and without retained foetal membranes.

Reproduction in Domestic Animals = Zuchthygiene
Monika FranczykM Kankofer

Abstract

The activity of glycosidases is crucial for the function and biological activity of proteins conjugated with sugar moieties, which play an important role in adhesion of cells during attachment and detachment of the foetal membranes. The aim of study was to describe the ability of bovine placental tissues to break down O-glycosidic bonds in different glycoproteins by the determination of activity of β-galactosidase, α-l-fucosidase, β-N-acetyl-hexosaminidase and sialidase in early-mid-pregnancy as well as at parturition with released and retained foetal membranes. Moreover, the availability of substrates for these glycosidases in placental homogenates was evaluated. Placental samples were collected from pregnant (2-4 months) cows in slaughterhouse (n = 8) as well as during Caesarean section and divided into released foetal membranes (n = 8) and retained foetal membranes (n = 8). Tissue homogenates were subjected to spectrofluorimetric and spectrophotometric determinations of enzyme activities as well as electrophoretic separations. Enzyme activities expressed changes within examined time with significant (p < .05) differences between pregnancy and physiological parturition in β-N-acetyl-hexosaminidase and α-l-fucosidase in foetal...Continue Reading

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Jul 20, 2018·Glycoconjugate Journal·Monika FranczykMarta Kankofer
Jul 31, 2019·Reproduction in Domestic Animals = Zuchthygiene·Jacek WawrzykowskiMarta Kankofer

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Citations

Feb 14, 2021·Reproduction in Domestic Animals = Zuchthygiene·Monika JamiołMarta Kankofer

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