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Electrophoretic-pOlarographic examination

Figure 7 is a representation of electrophoretic-polarographic examinations of a healthy person and of two patients suffering respectively from lipoid nephrosis and severe hepatitis. [Pg.467]

Figure 7. Electrophoretic-polarographic examination (a) top graph, healthy subject (6) middle graph, patient with lipoid nephrosis (c) bottom graph, patient with severe lesion of hepatic parenchyma. Figure 7. Electrophoretic-polarographic examination (a) top graph, healthy subject (6) middle graph, patient with lipoid nephrosis (c) bottom graph, patient with severe lesion of hepatic parenchyma.
The decrease in the content of albumin and increase in that of gamma globulin are more conspicuous in the electrophoretic-polarographic examination than in the staining method. The other fractions are altered as well. [Pg.469]

The feasibility of a separation of human albumin into two types, having respective molecular weights 67,000 and 134,000, of which the monomer does not contain titratable sulfhydryl groups and the dimer has two molecules of mercaptalalbumin derived from the intermolecular formation of disulfide, could be a starting point for further study of structural changes in albumin apprehensible by the electrophoretic-polarographic examination. [Pg.481]

Figure 8. Electrophoretic-polarographic denaturation examination of healthy subject. Figure 8. Electrophoretic-polarographic denaturation examination of healthy subject.
Let us now discuss the electrophoretic-polarographic denaturation examination of diseased subjects. [Pg.476]

Figure 14. Simplified electrophoretic-polarographic denaturation examination (a) before, (6) after denaturation. Albumin in both cases three times diluted. Figure 14. Simplified electrophoretic-polarographic denaturation examination (a) before, (6) after denaturation. Albumin in both cases three times diluted.
Normal Values for Electrophoretic-Polarographic Denaturation Examinations... [Pg.484]

Figure 31. Electrophoretic-polarographic denaturation examination marking of fractions on unstained electropherogram strip, a simple procedure. Figure 31. Electrophoretic-polarographic denaturation examination marking of fractions on unstained electropherogram strip, a simple procedure.
This is illustrated by Fig. 25, where media with various final values of pH were used (from the left) 3.4, 3.6, 3.7, 3.8, 3.9, 4.0 and 4.2 it is apparent that the range 3.7-3.9 is satisfactory. Just as in the examinations of pepsinogen, we also added cathepsin to electrophoretic protein fractions, and here the same result was obtained, showing that albumin is the principal fraction subject to polarographically detectable cleavage. We believe that the explanation is the same as that valid for pepsinogen, as described in Section 11. [Pg.514]


See other pages where Electrophoretic-pOlarographic examination is mentioned: [Pg.435]    [Pg.436]    [Pg.463]    [Pg.466]    [Pg.467]    [Pg.524]    [Pg.524]    [Pg.528]    [Pg.535]    [Pg.435]    [Pg.436]    [Pg.463]    [Pg.466]    [Pg.467]    [Pg.524]    [Pg.524]    [Pg.528]    [Pg.535]    [Pg.471]    [Pg.476]    [Pg.483]    [Pg.518]    [Pg.485]   
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