scholarly journals Chemical modification of carboxyl groups in porcine pepsin

1980 ◽  
Vol 28 (4) ◽  
pp. 834-839 ◽  
Author(s):  
Ching-Yung Ma ◽  
Shuryo Nakai
1974 ◽  
Vol 10 (6) ◽  
pp. 856-856
Author(s):  
D. I. Gorodetskii ◽  
N. F. Myasoedova ◽  
V. M. Stepanov

1981 ◽  
Vol 36 (9-10) ◽  
pp. 863-868 ◽  
Author(s):  
Matti Vuento ◽  
Eija Salonen

Abstract Purified hum an plasm a fibronectin has been shown to agglutinate protease-treated red cells [Vuento, Hoppe-Seyler's Z. Physiol. Chem. 360, 1327-1333, (1979)]. The present report shows that the activity is inhibited by low concentrations of lectins and by macrom olecular serum factors. Chemical m odification of carboxyl groups of fibronectin strongly inhibited the activity, but modification of am ino groups or guanidinium groups had little effect on the activity. The results suggest that fibronectin receptors on erythrocyte surface are carbohydrate-containing molecules. Humoral m acrom olecular factors may control the interaction of fibronectin with cell surfaces. Chemical m odification studies indicate that the parts of the fibronectin molecule responsible for the hem agglutinin activity are different from those mediating the binding of fibronectin to collagen.


1980 ◽  
Vol 17 (3) ◽  
pp. 327-336 ◽  
Author(s):  
F. Vivanco-Martínez ◽  
R. Bragado ◽  
J.P. Albar ◽  
C. Juarez ◽  
F. Ortíz-Masllorens

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