There are only a few reports concerning analyses of the protein components in the uterine cervical fluid. This is probably related to the difficulties of collecting the cervical fluid continuously and in significant amounts. In order to solve these problems, we developed a simple filter-disc-absorption method. Cervical fluid (CF) was adsorbed by a Whatman GF/B glass fiberdisc. It was then applied directly to the electrophoresis. Using this method, protein fractions and phosphorylase or lactate dehydrogenase isoenzymes in the CF of various gynecological states were investigated.
1. The CF from pregnant women in the first trimester as well as normal cycle shows weak protein fractions. As the pregnancy progress, especially after 30 gestational weeks, albumin and prealbumin levels are increased.
2. The CF obtained from patients with myoma of the uterine body and cancer of the uterine cervix contains a large amount of protein in comparison with that obtained from pregnant or normal cycle women. The electrophoretic pattern in the former cases resembles that of serum protein, especially in the cases with high protein content. However, no characteristic electrophoretic patterns which could be used to determine diseases or their severity were demonstrated.
3. Two phosphorylase bands were evident in CF from patients with the myoma and cancer. We called them the fast and the slow migrating phosphorylare bands (F-band and S-band). In the cases of cancer, the S-band was predominant, while in the cases of myoma, the F-band predominated. From these results, it was suggested that the distribution of the two phosphorylases could be used to differentiate between myoma and cervical cancer.
4. The distribution of LDH isoenzyme in the CF and in the serum of the same woman was different. The activities of LDH₁, LDH₂, LDH₃ isoenzymes were greater in the CF than in the serum. However, characteristic LDH-isoenzyme patterns of CF for typical gynecological diseases can not be determined.

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In my previous paper, I reported a simplified filter-disc-absorption method for analysis of cervical fluids. With this method, electrophoretic distributions of phosphorylase activities in cervical fluids were investigated.
1) Cervical fluid (CF) contained two phosphorylase isoenzymes with different mobilities: the fast moving (F-band) and the slow moving (S-band) phosphorylases. In the CF's obtained from women during a normal menstrual cycle and in normal pregnancy at the first and the middle gestational stages and from patients with myoma, the F-band isoenzyme appeared more frequently than the S-bands. In cases of which the CF contained both F-band and S-band, the former activity was much higher than the latter. In CF's of pregnant women during the last gestational stage, the S-band was more intense than the F-band. With advancement of the cancer, the S-band activity became more evident in the CF.
2) F- and S-bands of phosphorylase isoenzymes had different affinities to glycegen. The dissociation constants (K) of the isoenzymes and glycogen complexes were calculated from the results obtained by means of the affinity electrophoresis. The average K values were found to be 0.077% for the F-band and 0.029% for the S-band. These results indicated that the S-band has a higher affinity to glycogen than the F-band.

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Purified method of CRP in large scale and physicochemical properties of purified CRP were studied.
Human CRP was isolated from pleural and ascitic fluids using procedure as follows; (NH₄)₂SO₄ fractionation, DEAF-cellulose (DE-52), and gel-filtration (Sephacryl S-200).
A sigle protein band was observed on disc electrophoresis and on immunoelectrophoresis suggested pure that CRP was isolated by the above procedure. It was found that the purified CRP was crystallized with ease in the process of concentration by ultra-filtration. On analytical ultracentrifugation, purified CRP was found to be 7.38 Sw₂₀.
From amino acid analysis, it was determined that amino acid components of this purified CRP agreeds with the result reported by Edelman et al..
Specific antibody activity of antiserum obtained from rabbits immunized by the purified CRP was confirmed by immunoelectrophoresis.

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