4-pyridoxic acid 5'-phosphate: a metabolite of pyridoxol in the rat.
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Biomedical subjects
Publications and source records attributed to S F Contractor.
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Human placental cathepsin D has been purified 6000-fold and its properties characterized. Its molecular weight has been ascertained to be 42 000 by gel filtration and 43 300 by analytical ultracentrifugation. SDS gel electrophoresis in the presence of beta-mercaptoethanol cleaves the enzyme into two polypeptides of molecular weights 28 200 and 14 400. The placental enzyme resembles cathepsin D isolated from other mammalian tissues in many of its properties, including pH optimum. The higher degree of purification has led to a shift in the isoelectric points of the three isoenzymes from those recorded by other authors. Antibodies raised against cathepsin D in rabbits inhibit it at pH 5.0, and the inhibition is almost 100 per cent with adequate concentrations of monospecific antibody.
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Placental villi of early and term human placentae were dissociated with trypsin and mixed cell cultures were established. The different cell types were identified and estimated over a 14-day culture period using antibodies to keratin and vimentin filaments and their capacity to phagocytose yeast. The three main cell types were found to be epithelial-, macrophage- and fibroblast-like cells. The epithelial-like cells can be further divided into the multinucleated and the small- and medium-sized round cells, and these are most likely to be derived from the trophoblast. The cellular composition of cultures were different for early and term placentae and also varied characteristically over the 14-day cultures period.