scholarly journals Effect of cross-linking between 82 beta 1 and 82 beta 2 lysyl residues on the kinetics of polymerization of deoxyhemoglobin S.

1982 ◽  
Vol 257 (13) ◽  
pp. 7525-7530
Author(s):  
K Kikugawa ◽  
T Asakura ◽  
K Adachi
Keyword(s):  
Cross Linking ◽  
Kinetics Of Polymerization ◽  
Beta 2 ◽  
Kinetics Of

scholarly journals Mechanism of regulation of actin polymerization by Physarum profilin.

1984 ◽  
Vol 98 (6) ◽  
pp. 1919-1925 ◽  
Author(s):  
K Ozaki ◽  
S Hatano
Keyword(s):  
Steady State ◽  
Dissociation Constant ◽  
Actin Polymerization ◽  
Dissociation Constants ◽  
Critical Concentration ◽  
Cross Linking ◽  
Kinetics Of Polymerization ◽  
Kinetics Of ◽  
Chemical Cross Linking

Physarum profilin reduces the rates of nucleation and elongation of F-actin and also reduces the extent of polymerization of actin at the steady state in a concentration-dependent fashion. The apparent critical concentration for polymerization of actin is increased by the addition of profilin. These results can be explained by the idea that Physarum profilin forms a 1:1 complex with G-actin and decreases the concentration of actin available for polymerization. The dissociation constant for binding of profilin to G-actin is estimated from the kinetics of polymerization of G-actin and elongation of F-actin nuclei and from the increase of apparent critical concentration in the presence of profilin. The dissociation constants for binding of Physarum profilin to Physarum and muscle actins under physiological ionic conditions are in the ranges of 1.4-3.7 microM and 11.3-28.5 microM, respectively. When profilin is added to an F-actin solution, profilin binds to G-actin which co-exists with F-actin, and then G-actin is dissociated from F-actin to compensate for the decrease of the concentration of free G-actin and to keep it constant at the critical concentration. At the steady state, free G-actin of the critical concentration is in equilibrium not only with F-actin but also with profilin-G-actin complex. The stoichiometry of 1:1 for the formation of complex between profilin and G-actin is directly shown by means of chemical cross-linking.

scholarly journals Kinetics of Cross-Linking of Peptidoglycan in Bacillus megaterium

1974 ◽  
Vol 249 (8) ◽  
pp. 2478-2482
Author(s):  
William D. Fordham ◽  
Charles Gilvarg
Keyword(s):  
Bacillus Megaterium ◽  
Cross Linking ◽  
Kinetics Of

scholarly journals Viscometric analysis of the gelation of Acanthamoeba extracts and purification of two gelation factors.

1980 ◽  
Vol 85 (2) ◽  
pp. 414-428 ◽  
Author(s):  
S D MacLean-Fletcher ◽  
T D Pollard
Keyword(s):  
Crude Extract ◽  
Cross Linking ◽  
Cross Link ◽  
Gelation Process ◽  
Optimum Ph ◽  
Kinetics Of ◽  
Low Shear

We have studied the kinetics of the gelation process that occurs upon warming cold extracts of Acanthamoeba using a low-shear falling ball assay. We find that the reaction has at least two steps, requires 0.5 mM ATP and 1.5 mM MgCl2, and is inhibited by micromolar Ca++. The optimum pH is 7.0 and temperature, 25 degrees-30 degrees C. The rate of the reaction is increased by cold preincubation with both MgCl2 and ATP. Nonhydrolyzable analogues of ATP will not substitute for ATP either in this "potentiation reaction" or in the gelation process. Either of two purified or any one of four partially purified Acanthamoeba proteins will cross-link purified actin to form a gel, but none can account for the dependence of the reaction in the crude extract on Mg-ATP or its regulation by Ca++. This suggests that the extract contains, in addition to actin-cross-linking proteins, factors dependent on Mg-ATP and Ca++ that regulate the gelation process.

The kinetics of polymerization of dioxolane

1965 ◽  
Vol 7 (1) ◽  
pp. 1-9 ◽  
Author(s):  
M. Kučera ◽  
J. Pichler
Keyword(s):  
Kinetics Of Polymerization ◽  
Kinetics Of

Kinetics of polymerization of styrene

1980 ◽  
Vol 2 (9) ◽  
Author(s):  
M.V. Pandya ◽  
D.D. Deshpande ◽  
N.M. Desai
Keyword(s):  
Kinetics Of Polymerization ◽  
Kinetics Of
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