Identification and Localization of Phosphoproteins in v-onc Transformed Fibroblasts by Means of Phosphotyrosine Antibodies

1985 ◽  
pp. 97-112
Author(s):  
P. M. Comoglio ◽  
D. Cirillo ◽  
M. F. Di Renzo ◽  
R. Ferracini ◽  
F. G. Giancotti ◽  
...  
1971 ◽  
Vol 246 (18) ◽  
pp. 5785-5790
Author(s):  
Charles V. Peery ◽  
George S. Johnson ◽  
Ira Pastan

2007 ◽  
Vol 213 (1) ◽  
pp. 212-220 ◽  
Author(s):  
Renaud Poincloux ◽  
Céline Cougoule ◽  
Thomas Daubon ◽  
Isabelle Maridonneau-Parini ◽  
Véronique Le Cabec

1986 ◽  
Vol 10 (3) ◽  
pp. 161-161
Author(s):  
P MARCHISIO ◽  
D CIRILLO ◽  
F GIANCOTTI ◽  
P COMOGLIO ◽  
G TARONE

1975 ◽  
Vol 19 (1) ◽  
pp. 21-32
Author(s):  
J.G. Collard ◽  
J.H. Temmink

Calculations of the density of Concanavalin A (Con A)-binding sites on normal and transformed fibroblasts have, as yet, been based on the unproven assumption that suspended cells are smooth spheres. We studied the surface morphology of suspended normal and transformed fibroblasts with scanning and transmission electron microscopes, and found a large difference in surface morphology between suspended normal and transformed 3T3 cells. When this difference in surface morphology was taken into account, the estimated cell surface area of normal 3T3 cells was approximately seven times larger than that of transformed 3T3 cells. Since equal numbers of 3H-Con A molecules are bound on normal and transformed cells, the density of Con A-binding sites is approximately seven times greater on transformed than on normal 3T3 cells. The difference in density of Con A-binding sites between normal and transformed fibroblasts might be sufficient to explain the difference in agglutination response, as originally suggested by Burger, and may also be the cause of the different degrees of clustering of Con A-binding sites on the plasma membrane of these cells.


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