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Biomedical subjects

J Mazurier

Publications and source records attributed to J Mazurier.

4 recordsLinked to original sources

Iron binding proteins and influx of iron across the duodenal brush border. Evidence for specific lactotransferrin receptors in the human intestine.

The ability of a range of homologous transferrin-like proteins to donate iron to pieces of human duodenal mucosa, was examined with an in vitro incubation technique. In contrast to serum transferrin and ovotransferrin, only lactotransferrin was able to yield its iron to intestinal tissue, but in an autologous system this protein was unable to donate iron to human reticulocyte preparations. Studies with 125I-labelled lactotransferrin and lactotransferrin dual-labelled with 59Fe and 125I, indicated that the intact protein is excluded from entry into the enterocytes. The experiments suggest that iron may be transported across the brush border after delivery to specific protein binding sites at the cell surface.

Animals

The temperature and pH-dependent transition of hen lysozyme. Characterization of two temperature-defined domains and of an N-acetylglucosamine (inhibitor)-insensitive form.

The previously described temperature and pH-dependent transition in the solid state of hen lysozyme was studied in solution. Experiment concerning the velocity of lysis of M. luteus by lysozyme and its behavior in presence of an inhibitor (GlcNAc) as well as a reinvestigation of the Arrhenius curves over a large range of pH, demonstrated the existence of two temperature-induced domains. An inhibitor-insensitive lysozyme form was characterized at 40 degrees (physiological temperature).

Acetylglucosamine

[Chromatographic fractionation and studies on microheterogenity of cow lactotransferrin prepared by an original procedure].

Authors describe an original procedure to prepare pure lactotransferrin from cow milk. Physicochemical properties of this lactotransferrin have been studied and compared with results from others. New data are presented: presence of fucose and N-acetylgalactosamine; C-terminal amino-acid identified with threonine. On the other hand, 4 fractions have been obtained by "DEAE-Sephadex" chromatography, study of which demonstrates that the microheterogeneity of the lactotransferrin depends on the carbohydrate moiety and especially on the N-acetylneuraminic acid content which varies from 0 to 2 residues.

Amino Acid Sequence