Permalloy inductor based instrument that measures the sedimentation constant of magnetorheological fluids

2003 ◽  
Vol 74 (7) ◽  
pp. 3566-3568 ◽  
Author(s):  
L. S. Chen ◽  
D. Y. Chen
Keyword(s):  
Magnetorheological Fluids ◽  
Sedimentation Constant

A method and device for measurement of a sedimentation constant of magnetorheological fluids

2000 ◽  
Vol 71 (6) ◽  
pp. 2476-2480 ◽  
Author(s):  
S. R. Gorodkin ◽  
W. I. Kordonski ◽  
E. V. Medvedeva ◽  
Z. A. Novikova ◽  
A. B. Shorey ◽  
...  
Keyword(s):  
Magnetorheological Fluids ◽  
Sedimentation Constant

EFFECT OF PROPYLTHIOURACIL ON THE IODINATION AND MATURATION OF RAT THYROGLOBULIN

1966 ◽  
Vol 53 (2) ◽  
pp. 271-285 ◽  
Author(s):  
Claude Simon ◽  
Marie Roques ◽  
Janine Torresani ◽  
Serge Lissitzky
Keyword(s):  
Single Injection ◽  
Freezing And Thawing ◽  
Isotopic Equilibrium ◽  
Sedimentation Constant

ABSTRACT The effect of propylthiouracil on the maturation of rat thyroglobulin in vivo has been investigated. Newly iodinated thyroglobulin dimer is labile to freezing and thawing. This observation has been used to interpret the findings in the present experiments. From experiments using rats in isotopic equilibrium with 125I, and treated with propylthiouracil or propylthiouracil and tri-iodothyronine and also given a single injection of 131I, the following conclusions were formulated 1) the appearance of iodinated S12 thyroglobulin monomer is due to the dissociation of labile iodinated thyroglobulin dimer and appears more readily if the dimer is poorly iodinated, 2) uniodinated thyroglobulin dimer is the most probable substrate for iodination in vivo, 3) maturation of thyroglobulin dimer (as shown by increasing sedimentation constant from 16—17 to 19) is accompanied by increasing amounts of iodine in the molecule, 4) it is not possible to say at present if iodination and iodothyronine formation is the cause or the consequence of thyroglobulin dimer maturation, 5) propylthiouracil might inhibit thyroglobulin maturation by decreasing iodine organification.

Effect of Compound Surfactants Modified Carbonyl Iron on Magnetorheological Fluids

2021 ◽  
Author(s):  
Jingzhen Cheng ◽  
Kuo Liu ◽  
Zuocai Zhang ◽  
Zhouqiao Wei ◽  
Yinghui Ma ◽  
...  
Keyword(s):  
Carbonyl Iron ◽  
Magnetorheological Fluids

scholarly journals CONCENTRATION AND PURIFICATION OF BACTERIOPHAGE

1938 ◽  
Vol 21 (3) ◽  
pp. 335-366 ◽  
Author(s):  
John H. Northrop
Keyword(s):  
Molecular Weight ◽  
Small Molecules ◽  
Specific Activity ◽  
Active Agent ◽  
Pure Substance ◽  
Solubility Curve ◽  
Denatured Protein ◽  
Sedimentation Constant ◽  
Rate Of Sedimentation ◽  
Living Organisms

1. A method for isolating a nucleoprotein from lysed staphylococci culture is described. 2. It is homogeneous in the ultracentrifuge and has a sedimentation constant of 650 x 10–13 cm. dyne–1 sec.–1, corresponding to a molecular weight of about 300,000,000. 3. The diffusion coefficient varies from about 0.001 cm.2/day in solutions containing more than 0.1 mg. protein/ml. to 0.02 in solutions containing less than 0.001 mg. protein/ml. The rate of sedimentation also decreases as the concentration decreases. It is suggested, therefore, that this protein exists in various sized molecules of from 500,000–300,000,000 molecular weight, the proportion of small molecules increasing as the concentration decreases. 4. This protein is very unstable and is denatured by acidity greater than pH 5.0, by temperature over 50°C. for 5 minutes. It is digested by chymo-trypsin but not by trypsin. 5. The loss in activity by heat, acid, and chymo-trypsin digestion is roughly proportional to the amount of denatured protein formed under these conditions. 6. The rate of diffusion of the protein is the same as that of the active agent. 7. The rate of sedimentation of the protein is the same as that of the active agent. 8. The loss in activity when susceptible living or dead bacteria are added to a solution of the protein is proportional to the loss in protein from the solution. Non-susceptible bacteria remove neither protein nor activity. 9. The relative ultraviolet light absorption, as determined directly, agrees with that calculated from Gates' inactivation experiments in the range of 2500–3000 Å. u. but is somewhat greater in the range of 2000–2500 Å. u. 10. Solubility determinations showed that most of the preparations contained at least two proteins, one being probably the denatured form of the other. Two preparations were obtained, however, which had about twice the specific activity of the earlier ones and which gave a solubility curve approximating that of a pure substance. 11. It is suggested that the formation of phage may be more simply explained by analogy with the autocatalytic formation of pepsin and trypsin than by analogy with the far more complicated system of living organisms.

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