scholarly journals Boundary spreading in sedimentation-velocity experiments. 4. Measurement of the standard deviation of a sedimentation-coefficient distribution: application to bovine albumin and β-lactoglobulin*

1957 ◽  
Vol 65 (3) ◽  
pp. 490-502 ◽  
Author(s):  
R. L. Baldwin
Keyword(s):  
Standard Deviation ◽  
Sedimentation Coefficient ◽  
Sedimentation Velocity ◽  
Bovine Albumin ◽  
Coefficient Distribution ◽  
Β Lactoglobulin

scholarly journals Nitrogenase of Klebsiella pneumoniae. Interaction of the component proteins studied by ultracentrifugation

1973 ◽  
Vol 135 (3) ◽  
pp. 531-535 ◽  
Author(s):  
Robert R. Eady
Keyword(s):  
Klebsiella Pneumoniae ◽  
Sedimentation Coefficient ◽  
Sedimentation Velocity ◽  
Single Peak ◽  
Molar Ratio ◽  
Titration Curves ◽  
Additional Peak

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).

PHYSICOCHEMICAL STUDIES OF ALKALI LIGNINS: II. ULTRACENTRIFUGAL SEDIMENTATION ANALYSIS

1960 ◽  
Vol 38 (2) ◽  
pp. 259-269 ◽  
Author(s):  
P. R. Gupta ◽  
R. F. Robertson ◽  
D. A. I. Goring
Keyword(s):  
Standard Deviation ◽  
Linear Relationship ◽  
Intrinsic Viscosity ◽  
Sedimentation Coefficient ◽  
Wide Distribution ◽  
Small Decrease ◽  
Sedimentation Analysis ◽  
Qualitative Interpretation ◽  
Physicochemical Studies ◽  
Lamm Equation

Ultracentrifugal sedimentation of alkali lignin fractions revealed marked boundary spreading at low and high centrifugal fields. An analysis of the gradient diagrams indicated a wide distribution of sedimentation coefficients ranging from 0.5 to over 400 × 10−13 second. There was only a small decrease in the polydispersity on subfractionation. The distributions were continuous with a single peak and positive skewness. A linear relationship was found between the intrinsic viscosity and the standard deviation of the weight-average sedimentation coefficient. The sedimentation coefficient based on the movement of the maximum ordinate at a field of 11.5 × 103 g was several times greater than the corresponding coefficient for the same fraction at 200 × 103 g. A qualitative interpretation of this phenomenon is given in terms of the Faxen and the Archibald solution to the Lamm equation.

Multiple Molecular Forms of Avian Aldolases. V. Purification and Molecular Properties of Chicken (Gallus domesticus) Liver Aldolase

1971 ◽  
Vol 49 (6) ◽  
pp. 647-657 ◽  
Author(s):  
Ronald R. Marquardt
Keyword(s):  
Molecular Weight ◽  
Specific Activity ◽  
Diffusion Constant ◽  
Sedimentation Coefficient ◽  
Sedimentation Velocity ◽  
Gallus Domesticus ◽  
Molecular Forms ◽  
Velocity Analysis ◽  
Multiple Molecular Forms ◽  
Stokes Radius

Aldolase (fructose-1,6-diphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) was purified from chicken liver. The enzyme was shown to be homogeneous according to the following criteria: purification to a constant specific activity following sequential chromatography on carboxymethyl-Sephadex and Sephadex G-200, electrophoresis on cellulose acetate strips, sedimentation velocity analysis, absence of 10 other glycolytic enzymes, and immunodiffusion in agar.The sedimentation coefficient (s°20w 8.0), Stokes radius (47 Å), diffusion constant (D°20w 4.0 × 10−7 cm2/s), and molecular weight (160 000) are similar to those of rabbit liver aldolase and the muscle and brain enzymes from both chickens and rabbits.

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