Sedimentation diagrams

Figure 7.4. A sedimentation diagram for a hypothetical Devonian-age carbonate sequence. The curve for the sequence gives its inferred position relative to sea level and land surface elevation since the time of its sedimentation. Schematic subsurface isotherms are also presented based on estimates of crustal thickness and hypothetical heat flow values related to plate movements and igneous activity. [Adapted from Siever s (1979) representation of the Esopus Formation.]...

The matrix possesses a specific conformation under the initial conditions (e.g. the PMAA-PEG system in water). At 0 < / < 1, i.e. if the matrix polymer is present in excess two peaks A and B appear in the sedimentation diagram. The velocity of sedimentation of the rapid fraction is practically the same as that of the polycomplex at P = 1. The slow fraction B sedimentates at a velocity which is characteristic of PMAA (/ = 0). Thus, the distribution of oligomer between the matrix molecules occurs according to the all-or-none principle, i.e. at 0 < / < 1 a part of the matrix polymer is completely bound and the others part is practically free. 

The matrix does not possess initially any specific conformation, e.g. the PAA-PEG system in water and the PMAA-PEG system in a methanol-water (ft) 40 vol-%) mixture. In this case, irrespective of the ratio of the components (i.e. of /3), only one peak appears in the sedimentation diagram. This confirms the statistical distribution of oligomers between the matrix molecules. 

Fig. 20 (78). Sedimentation diagram of bovine apoerythrocuprein. The protein concentration was 2.1 mg and 4.1 mg dissolved in 5 mM phosphate buffer, pH 7.2. Direction of sedimentation left to right, speed 60,000 rpm. Schlieren bar angle 50°, 12 mm Al-valve synthetic boundary cell. Photographs were taken at 16-min intervals after reaching full speed...

A particular advantage of the sedimentation-velocity technique is that a macro-molecular solution containing more than one type of molecule is separated according to the molecular masses of the components. Figure 11.156 shows the type of sedimentation diagram obtained for a system containing a number of components. 

The sedimentation diagrams of Fig. 21 are also indicative of a monodisperse substance. The curve with open circles represents the theoretical spreading of the peak between Xi and xio due to diffusion, as calculated from the diffusion constant at that particular concentration (0.64 X 10 ... 

Figure 8.4 Sedimentation diagrams of polymeric species, (a) Initial polystyrene (b) fraction 3 with nanosponges (c) fraction 2 with clusters (d) a 1 1 mixture of clusters and nanosponges. Solvent chloroform, 25°C. Rotation rates (mln" ) (a) 40,000, (b) 36,000, (c) 16,000, (d) 25,000. (Reprinted from [239] with permission of Wiley Sons, Inc.)...

To confirm a cooperative destruction of PEC particles near the lEP, independent sedimentation experiments were carried out. Figure 32 shows the sedimentation diagrams of DMVEP-AA, PAA and PEC at various pH. The sedimento-grams of PEC show one peak with S=4.75 and 4.18 at pH=6.1 and 6.9, respectively. However at pH=7.1 two peaks with S=1.9 ( slow peak) and 5.6 ( fast peak) appear on sedimentograms. At the same time the sedimentation coefficients of separate components DMVEP-AA and PAA at pH=7.2 are equal to 3.53 and 1.06, respectively. 

Fig. 2. Sedimentation diagrams of D-RNA-containing nuclear extracts from rat liver nuclei A.) Obtained in the absence of RNase inhibitor (animals injected with 32porthophosphate and C amino acids). Curves A-optical density B-labeled RNA ( P) C-labeled protein( C).

Fig. 7. Sedimentation diagrams of nuclear extract (upper curve) and D-RNAs isolated from different zones of nuclear extract (lower curves). A. 308 B. 45S C.60S D. 75S E. 120 to 130S. Ultracentrifugation of RNAs was carried out in the presence of nonlabled carrier (cytoplasmic RNA containing 28S and 18S peaks) in the SW-39 rotor 5 to 20 percent sucrose gradient in 0.05 M NaCI - 0.005 M EDTA - 0.25 percent SDS - 0.01 M tris (pH 7.5) 35,000 rpm, 4 hours, 20°C. Solid lines, radioactivities dotted line, U. V. absorption of marker. (From Samarina et al. 1968a. J. Molec. BioL, 33 251-263.)...

McFarlane, a. S. Ultracentrifugal protein sedimentation diagram of normal human, cow and horse serum. Biochem. J. 29, 660—693 (1935). 

Fig. 2. (Comparison of the theoretical diffusion curves and actual sedimentation diagrams for E. colt bacteriophage T6 at pH 4.9. The solid line curves represent the mean ordinate of the sehlieren curve (corrected for camera magnification) and the circles denote the theoretical boundary diagram calculated from the diffusion constant. The position of the meniscus is given by the vertical arrow. Curves are given for 6280, 7200, and 10,080 seconds after the beginning of acceleration to 3150 r.p.m. (255).

Fig. 13. Sedimentation of fumsraae in the presence of thiocyanate. Sedimentation diagrams of a 0.45 % solution of fumarase in the presence of 0.05 M phosphate pH 7.4 and 0.1 M NH,CNS. (From studies of V. Massey and P. Johnson.)...

Fig. 7 represents in schematic form a sedimentation diagram obtained with normal adult human serum under standardized conditions (276). Four components are indicated, the largest, 820 approximately 4.5, is designated A and consists chiefly of albumins another, 820 approximately 7 S, is designated G and consists largely of various globulins a rapidly sedimenting component, S20 between 175 and 20 8, was found upon electro-... 

The ultracentrifuge has found comparatively little application to the study of pathological sera. McFarlane (235) obtained sedimentation diagrams of the sera in patients with tuberculosis, pneumonia, scarlet fever, multiple myeloma, ovarian carcinoma, and other disorders, but the results proved difiUcult to interpret. He found evidence of an increase in globuhns in some of the infections and in one case of myeloma noted a large fraction (probably not the X-protein), intermediate in sedimentation rate between the A and G components. Interesting results have been obtained in multiple myeloma (162, 178, 233, 235, 251, 271) in efforts to identify Bence-Jones proteins in the blood and urine. Whereas typical Bence-Jones proteins obtained from the urine (235, 251,... 

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