sambucus williamsii/atrophy

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AtikEsè klinikPatant

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3 rezilta yo

Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Sträussler-Scheinker disease.

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Prion diseases are caused by an abnormal form of the prion protein (PrP(Sc)). We identified, with lectins, post-translational modifications of brain proteins due to glycosylation in a Gerstmann-Sträussler-Scheinker (GSS) patient. The lectin Amaranthus leucocarpus (ALL), specific for mucin type

Alterations in molecular status of plasma fibronectin associated with aging of normal human individuals.

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OBJECTIVE Senescence, progressive deterioration of many bodily functions might be associated with age-dependent alterations of plasma fibronectin (FN) molecular status (i.e., domain, glycotope, and molecular form expressions). METHODS FN molecular status was analyzed in 127 plasma samples of healthy

Glycosylation pattern and enzyme activities in atrophic, angulated skeletal muscle fibres from ageing rats.

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In this study enzyme activities and lectin binding patterns in skeletal muscle from very old rats were investigated in order to evaluate changes in enzyme activity or carbohydrate expression in senile muscle. Activities for adenosine triphosphatase (ATPase), succinic dehydrogenase, non-specific

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