The relationship of the cell surface to metabolism. I. Phosphatases in the cell surface of living yeast cells

1948 ◽  
Vol 32 (1) ◽  
pp. 77-95 ◽  
Author(s):  
Aser Rothstein ◽  
Rebecca Meier
Keyword(s):  
Cell Surface ◽  
Yeast Cells ◽  
Relationship Of ◽  
The Relationship

scholarly journals SIMILARITY OF THE KINETICS OF INVERTASE ACTION IN VIVO AND IN VITRO. III

1933 ◽  
Vol 16 (4) ◽  
pp. 571-577 ◽  
Author(s):  
J. M. Nelson ◽  
B. G. Wilkes
Keyword(s):  
Physiological Activity ◽  
Water Concentration ◽  
Invertase Activity ◽  
Yeast Cells ◽  
Identical Manner ◽  
A Cell ◽  
Relationship Of ◽  
The Relationship

1. The relationship of sucrose and water concentration to invertase activity in vivo and in vitro has been studied under the same environmental conditions. 2. The sucroclastic activity of S. cerevisiae cells and of invertase solutions prepared from them reacts to changes in sucrose and water concentration in an identical manner. 3. The invertase contained in living yeast cells is just as freely exposed to the conditions of sucrose and water concentrations of the suspending medium as it would be if it were contained in a cell-free solution. Weight is added to the previous suggestion (2) that yeast invertase exerts its physiological activity in a region quite close to the surface of the cell.

scholarly journals Expression of a new cell surface antigen on activated murine macrophages.

1977 ◽  
Vol 146 (5) ◽  
pp. 1461-1466 ◽  
Author(s):  
A M Kaplan ◽  
T Mohanakumar
Keyword(s):  
Cell Surface ◽  
Surface Antigen ◽  
Rabbit Antiserum ◽  
Cell Surface Antigen ◽  
Macrophage Cell ◽  
Murine Macrophages ◽  
Cell Surface Changes ◽  
Relationship Of ◽  
The Relationship

A macrophage cell-surface antigen associated with pyran and Corynebacterium parvum-activated macrophages and P388D1 cells but not detectable on normal or glycogen and thioglycollate-elicited murine macrophages has been described. The antigen was demonstrated both by complement-mediated cytotoxicity and immunofluorescence, using an appropriately absorbed rabbit antiserum to P388D1. This antiserum should enable the characterization of activated macrophage cell populations on an individual cell basis and should be a useful probe to study the interactions of macrophages with tumor cells and the relationship of activation to cell-surface changes.

scholarly journals THE RELATIONSHIP OF CONCANAVALIN A BINDING TO LECTIN-INITIATED CELL AGGLUTINATION

1973 ◽  
Vol 59 (1) ◽  
pp. 134-142 ◽  
Author(s):  
Kenneth D. Noonan ◽  
Max M. Burger
Keyword(s):  
Cell Surface ◽  
Concanavalin A ◽  
Room Temperature ◽  
Transformed Cells ◽  
Glutaraldehyde Fixation ◽  
Cell Agglutination ◽  
Normal Cells ◽  
Receptor Sites ◽  
Relationship Of ◽  
The Relationship

We have investigated the relationship of concanavalin. A binding to the cell surface of normal and transformed cells and the subsequent agglutination of the transformed cells. At room temperature almost no differences could be detected in agglutinin binding between transformed and untransformed cells. At 0°C, however, where endocytosis was negligible, the transformed cells bound three times more agglutinin. However, transformed cells and trypsin-treated normal cells do not agglutinate at 0°C although the amounts of agglutinin bound at 0°C are sufficient to permit agglutination when such cells are shifted up to room temperature. Both transformed and trypsin-treated normal cells show a marked increase in agglutination at 15°C as compared to agglutination at 0°C. From this, as well as the observation that mild glutaraldehyde fixation of the cell surface inhibited agglutination but not agglutinin binding, it was concluded that concanavalin A-mediated cell agglutination requires free movement of the agglutinin receptor sites within the plane of the cell surface.

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