Light-scattering study of the effect of sodium chloride on the molecular weight of human adult hemoglobin

Biochemistry ◽  
1971 ◽  
Vol 10 (17) ◽  
pp. 3222-3229 ◽  
Author(s):  
Chien Ho ◽  
Ingrid B. E. Noren ◽  
Edward F. Casassa
1978 ◽  
Vol 8 (2) ◽  
pp. 133-138 ◽  
Author(s):  
M.Constance Loeffler ◽  
Shian-shi Su ◽  
Norman C. Li ◽  
Edward F. Casassa

1950 ◽  
Vol 28b (3) ◽  
pp. 96-104 ◽  
Author(s):  
D. B. Smith ◽  
H. Sheffer

The scattering of light by aqueous solutions of three different samples of sodium thymonucleate has been investigated. It was found that one sample in water consisted of randomly coiled molecules of molecular weight greater than 24 × 106. A second sample gave a less viscous solution in water and was only partially coiled, the coiling of the molecules being increased by the addition of a small amount of sodium chloride. In dilute salt solution the molecular weights of all three samples were greater than 3.7 × 106. Two samples of nucleate were degraded in solution by irradiation with ultraviolet light in the presence of hydrogen peroxide. In both cases the nucleate was converted into material consisting of rodlike molecules, 2400 Å in length and having a molecular weight of 750,000.


1958 ◽  
Vol 36 (11) ◽  
pp. 1584-1595 ◽  
Author(s):  
A. E. Leger ◽  
J. C. Hyde ◽  
H. Sheffer

A light-scattering study of aluminum distearate in dilute benzene solution suggests that it is a linear molecule of random coil shape. This is further substantiated by intrinsic viscosity – molecular weight data, the constancy of the ratio of the molecular weight to the square of the radius of gyration (Rg), the value of Φ in Flory's intrinsic viscosity – molecular weight relationship, and the close agreement between the theoretical and experimental results found for the unit length of the polymer chain. This average unit length has been calculated to be 4.46 Å.


1956 ◽  
Vol 34 (2) ◽  
pp. 160-169 ◽  
Author(s):  
M. E. Reichmann ◽  
J. Ross Colvin

The molecular weight of performic acid oxidized bovine plasma albumin, dispersed in 0.08 M borate +0.2 M sodium chloride buffer, pH 7.4, was estimated as 30,000 by light-scattering and sedimentation equilibrium methods, 19,000 by osmotic pressure. Sedimentation velocity analyses and electrophoresis showed that the component polypeptide chains of the material are similar in mass and charge density so the polydispersity must be attributed to labile aggregates. The results indicate that here are at least three and probably four similar polypeptide chains in the molecule of native bovine plasma albumin, held together by disulphide bonds.


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