The sialic acids. XV. Transfer of sialic acid to glycoproteins by a sialyltransferase from colostrum.
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Biomedical subjects
Publications and source records attributed to S Roseman.
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Intercellular adhesion is measured by a new method based on determination of the rates of attachment of single cells to confluent cell monolayers. The procedure is simple, rapid, and reproducible. Specific and nonspecific intercellular adhesions can be quantitated and distinguished from each other, and from the adhesion to glass (or plastic). The rate of adhesion of single cells to the monolayer is characteristic of more than 80% of the single-cell population. This method, therefore, provides a means for study of the molecular basis of intercellular adhesion.
Animal cells are coated with complex carbohydrates. Insoluble analogues of these substances were prepared by coupling monosaccharides to Sephadex beads (crosslinked dextran), and the interactions between these derivatives and three established cell lines were studied. A virally transformed fibroblast, simian virus 40-transformed 3T3 cells, adhered to the beads derivatized with D-galactose, but did not adhere to the corresponding beads derivatized with D-glucose or N-acetyl-D-glucosamine. Cells that adhered to the galactose-beads appeared to initiate a nucleation process in that they became more adhesive towards the cells in suspension, leading to the formation of large aggregates containing both cells and galactose-beads. The results suggest that specific carbohydrates are involved in the processes of cell recognition or cell adhesion, or both.
Salmonella typhimurium strains, lacking both enzyme I and the phosphocarrier protein, HPr, of the phosphoenolpyruvate-sugar phosphotransferase system, cannot transport or metabolize glucose and other sugar substrates of this enzyme system. Mutants which regain the ability to specifically utilize glucose were found to constitutively synthesize a galactose permease by virtue of a mutation in the galR gene. This permease, shown to be an active transport system, does not require HPr or enzyme I for activity.
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Sugars transported by a bacterial phosphoenolpyruvate:sugar phosphotransferase system (PTS) require two soluble proteins: HPr, a low-molecular-weight phosphate-carrier protein, and enzyme I. The structural genes coding for HPr (ptsH) and Enzyme I (ptsI) are shown to be cotransducible in Salmonella typhimurium. The gene order of this region of the Salmonella chromosome is cysA-trzA-ptsH-ptsI...(crr). A method for the isolation of trzA-pts deletion is described. One class of pts deletions extends through ptsH and into ptsI; a second class includes both ptsH and ptsI and extends into or through the crr gene. The crr gene either codes for or regulates the synthesis of a third PTS protein (factor III) which is sugar-specific. A hypothesis is presented for a mechanism of deletion formation.
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