scholarly journals A Method for Directly Fitting the Time Derivative of Sedimentation Velocity Data and an Alternative Algorithm for Calculating Sedimentation Coefficient Distribution Functions

2000 ◽  
Vol 279 (2) ◽  
pp. 151-163 ◽  
Author(s):  
John S. Philo
2013 ◽  
Vol 437 (2) ◽  
pp. 133-137 ◽  
Author(s):  
Daniel F. Lyons ◽  
Jeffrey W. Lary ◽  
Bushra Husain ◽  
John J. Correia ◽  
James L. Cole

1973 ◽  
Vol 135 (3) ◽  
pp. 531-535 ◽  
Author(s):  
Robert R. Eady

Sedimentation-velocity analyses of mixtures of the component proteins of nitrogenase of Klebsiella pneumoniae at a 1:1 molar ratio, showed a single peak of sedimentation coefficient (12.4S) considerably greater than that obtained for the larger (Fe+Mo-containing) protein centrifuged alone (10.4S). When the ratio exceeded 1:1 (the smaller Fe-containing protein in excess) an additional peak corresponding in sedimentation coefficient (about 4.5S) to free Fe-containing protein appeared. When proteins, which had been inactivated by exposure to air were used, no interaction occurred. Na2S2O4 at 2mm both reversed and prevented interaction between the two proteins; sedimentation coefficients corresponded to those of the proteins when centrifuged alone. These results demonstrate the formation of a complex between the nitrogenase proteins, and, together with data of activity titration curves, are consistent with the formulation of the nitrogenase complex of K. pneumoniae as (Fe-containing protein)–(Fe+Mo-containing protein).


2010 ◽  
Vol 10 (7) ◽  
pp. 736-745 ◽  
Author(s):  
Huaying Zhao ◽  
Patrick H. Brown ◽  
Andrea Balbo ◽  
María del Carmen Fernández-Alonso ◽  
Natasha Polishchuck ◽  
...  

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