• Biomedical Science Letters
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• v.16 no.1
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• pp.19-24
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• 2010

We analyzed and compared the concentration of total cholesterol (CHOL), high density lipoprotein (HDL) cholesterol, low density lipoprotein (LDL) cholesterol and triglyceride (TG) in serum and the serum protein electrophoresis fractions of thyroid disease patients. In comparison with the average of reference, our data showed that the average concentration of CHOL, LDL cholesterol and TG in hyperthyroidism patients were decreased significantly, but HDL cholesterol was increased significantly. In hypothyroidism patients, CHOL, HDL cholesterol, LDL cholesterol and TG were all increased significantly. In comparison of the concentration of lipids in each patient to reference range, 28.3% of hyperthyroidism patients showed abnormally low level of total cholesterol. In the patients with hypothyroidism, the percentage of patients showed abnormally high level of CHOL, HDL cholesterol, LDL cholesterol and TG were 37.7%, 10%, 68.8% and 49.1%, respectively. In our studies of serum protein electrophoresis, the average of ${\alpha}_2$-globulin and $\gamma$-globulin in hyperthyroidism patients were increased and $\beta$-globulin was decreased significantly. In hypothyroidism patients, the average of $\gamma$-globulin was increased and $\beta$-globulin was decreased significantly. In comparison of protein fractions of each patient to reference range, 38.3% and 50.0% of hyperthyroidism patients showed abnormally high levels of ${\alpha}_2$-globulin and $\gamma$-globulin, but 73.3% of patients showed abnormally low level of $\beta$-globulin. In hypothyroidism patients, 70.4% of patients were abnormally decreased in $\beta$-globulin and 63.9% of patients were abnormally increased in $\gamma$-globulin. These data suggest that the concentrations of CHOL, HDL cholesterol, LDL cholesterol and TG are not critical data for clinical interpretation of hyperthyroidism, but the levels of them are useful for interpretation of hypothyroidism patients. Our results of serum protein electrophoresis suggest that the concentration of serum protein electrophoresis fractions can be useful to understand the thyroid disease.

• Korean Journal of Veterinary Research
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• v.5 no.1
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• pp.1-16
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• 1965

I. A Comparison of Sodium Sulfate Precipitation and Zone(Paper, Agar) Electrophoresis; Many kinds of techniques have been used for fractionating serum proteins. In the present study, using bovine serum, the fractions obtained with sodium sulfate were compared with those determined by zone electrophoresis. 1. Fibrinogen was precipitated with 4 to 10 percent of sodium sulfate. 2. ${\gamma}$-globulin required 10 to 16 percent of the salt for precipitation. 3. ${\beta}$-globulin began to precipitate at 12 percent sodium sulfate, and completed precipitation at approximately 26 percent in paper electrophoresis, while at 22 percent in agar electrophoresis. 4. ${\alpha}$-globulin completed precipitation at 13 to 28 percent sodium sulfate in paper electrophoresis and at 22 percent in agar electrophoresis. 5. Albumin began to precipitate at 14 percent of the salt, and was free from the mixture of globulins approximately at 28 percent in paper electrophoresis, while at 22 percent in agar electrophoresis. The results of comparing fractions by the two methods were as follows: 1. Euglobulin (15%) was equal to the sum of the most ${\gamma}$-globulin and a small quantity of the ${\alpha}$-, and ${\beta}$-globulins. 2. Pseudoglobulin I (15-17.5%) corresponded to the most ${\alpha}$-, ${\beta}$-globulins and a small quantity of albumin. 3. Pseudoglobulin II(18-22%) was a mixture of the ${\alpha}$-, ${\beta}$-globulins and albumin fraction. 4. Albumin (above 22%) contained the most albumin fraction separated by zone electrophoresis and a small quantity of the ${\alpha}$-, and ${\beta}$-globulins. As mentioned above the fractions obtained with sodium sulfate were a mixture of the various proportion of the fractions determined by zone electrophoresis. The solubility of serum fractions to sodium sulfate coincided with the mobility of those by zone electrophoresis. (By percent of sodium sulfate we mean gram of sodium sulfate contained in $100m{\ell}$ of solution). II. Immunological Studies on Serum Protein Fractions with Sodium Sulfate; In the previous report the fractions of bovine serum protein with sodium sulfate compared with those obtained by zone electrophoresis, and the findings were that the former contained various proportion components of the latter. In this study the author studied whether or not the fractions with sodium sulfate are simple component antigenically by immunoelectrophoresis and micro double diffusion test (Immuno-precipitation), using rabbit antiserum to bovine serum. In immunoelectrophoresis, normal bovine serum developed with rabbit antibovine serum showed about ten distinct precipitin arcs. The distribution of these arcs was as follows: 1 albumin, 2 ${\alpha}_1$-, 3 ${\alpha}_2$-, 2 ${\beta}_1$-, ${\beta}_2$-, and 1 ${\gamma}$-globulin (Fig. 7, 9). In micro double diffusion test, five to six precipitation bands could be seen between antigens and antibody, the order of the precipitation bands location is albumin, ${\alpha}$-, ${\beta}$-, and ${\gamma}$-globulin from the side of antiserum well (Fig.19). Frequently the ${\alpha}$-, and ${\beta}$-precipitation bands were separated into two or three precipitation bands, which indicated that these globuline are not a pure component antigenically as shown in immuno-electrophoresis. In both Immunological methods, the two ${\alpha}$-, ${\beta}$-precipitin arcs and bands appeared clear and strong, indicating that the two globulins reacted as strong antigens. The precipitate reaction of ${\gamma}$-globulin was shown at 12 to 16 percent sodium sulfate; ${\beta}$-globulin at 12 to 20 percent; ${\alpha}$-globulin at 12 to 22 percent (immuno-electrophoresis), at 12 to 26 percent (Diffusion); and albumin at above 22 percent. Antigenically euglobulin contained ${\gamma}$-, ${\beta}$-, and ${\alpha}$-globulins, Pseudoglobulin I and Pseudoglobulin II were composed of ${\alpha}$-, and ${\beta}$-globulins, and albumin was a mixture of ${\alpha}$-globulin and albumin determined by zone electrophoresis. The results indicated that the fractions of serum protein obtained by either method were constituents of various proteins antigenically except ${\gamma}$-globulin and albumin by Zone electrophoresis.

• Korean Journal of Veterinary Service
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• v.33 no.3
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• pp.293-297
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• 2010

Serum proteins of Korean native dogs (Gyeongju DongGyeong dogs) was analyzed by capillary electrophoresis system. Electrophoretic patterns showed six fractions. Total serum protein and ratio of albumin to globulin were $5.99{\pm}0.83$ (g/dl) and $1.41{\pm}0.29$ (g/dl) in DongGyeong dogs. Relative percentages of total serum albumin and $\alpha-1$, $\alpha-2$, $\beta-1$, $\beta-2$, $\gamma$-globulin fraction were $57.94{\pm}5.43$, $3.15{\pm}2.30$, $7.49{\pm}4.09$, $9.43{\pm}3.50$, $7.63{\pm}5.70$, and $14.36{\pm}7.63$, respectively. It was observed that $\beta$-globulin was higher than other fractions. The most striking alternation with age was founded in the $\gamma$-fractions. Also, it was observed that ratios of albumin to globulin in DongGyeong dogs were higher than on other dogs.

• Korean Journal of Clinical Laboratory Science
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• v.37 no.2
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• pp.61-64
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• 2005

We compared the serum protein electrophoresis patterns in sera of diabetes patients (n=166) which showed more than 150 mg/dL of glucose. The concentrations of total protein, albumin, ${\alpha}1$-globulin, ${\alpha}2$-globulin, ${\beta}$-globulin and ${\gamma}$-globulin in sera of patients were $6.3{\pm}1.2g/dL$, $40.3{\pm}6.4%$, $4.9{\pm}2.3%$, $13.5{\pm}3.8%$, $15.5{\pm}3.9%$, and $25.9{\pm}5.8%$, respectively. The frequency of patients showed lower levels of total protein, albumin, ${\alpha}1$-globulin were 48.5%, 96.4%, and 33.7%. The frequency of patients showed higher levels of ${\alpha}2$-globulin, ${\beta}$-globulin, and ${\gamma}$-globulin were 56.6%, 47.0%, and 90.4%, respectively. This data suggests that the high concentration of glucose in blood may damage the kidney and liver. Also, the decrease of albumin and ${\alpha}1$-globulin and increase of ${\alpha}2$-globulin, ${\beta}$-globulin and ${\gamma}$-globulin shows that the concentration of glucose in blood will have an effect on the variation of serum protein electrophoretic patterns.

• Korean Journal of Veterinary Research
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• v.31 no.1
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• pp.99-108
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• 1991

To observe the changes of serum proteins according to the process of Babesia gibsoni(B gibsoni) infection, the babesia protozoa($10^8/kg$) were inoculated into the cephalic vein of healthy dogs. The serum proteins of experimentally infected dogs were separated by using cellulose acetate electrophoresis. The results obtained were as follows; 1. Cellulose acetate electrophoresis was fractionated to total 6 of bands such as, albumin, ${\alpha}_1$, ${\alpha}_2$, ${\beta}_1$, ${\beta}_2$ and $\gamma$-globulin. 2. The concentration of total protein was shown a decreasing tendency after B gibsoni infection. Albumin and A/G ratio were lowered through all periods of the infection, but they were not significant changes. 3. The level of ${\alpha}_1$-globulin was significantly(p<0.05) incresed in early stage of the infection. 4. The levels of ${\alpha}_2$ and total $\alpha$-globulin were shown highly significant decreases (p<0.01) through all periods of the infection. 5. The levels of ${\beta}_1$ and total $\beta$-globulin had highly significant changes (p<0.01) that was increased in early stage of infection and decreased later. 6. The level of $\gamma$-globulin was seen to be constantly increased through all periods of infection. It was a highly significant change (p<0.01). 7. Plasma protein: fibrinogen (PP:F) ratio was shown a temporally significant increase (p<0.05) following the decrease in early infection.

• Restorative Dentistry and Endodontics
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• v.2 no.1
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• pp.20-26
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• 1976

Cellulose acetate electrophoresis was used for differential diagnosis of radicular cysts and granulomas. Sixteen periapical lesions were excised from sixteen teeth with radiographic evidence of periapical pathosis, and two normal periodontal tissues were surgically removed from two wisdom teeth. The tissue samples were separated into two parts. Half was prepared for cellulose acetate electrophoresis, and the electrophoretic patterns were scanned with Helena densitometer. The other half was examined histologically, and the histologic diagnoses were then compared with the electrophoretic patterns and with the x-ray findings. The results were the following: 1. The histopathologic results showed the presence of 13 granulomas (81.8%) and 3 cysts (18.3%). 2. An albumin pattern, alpha-globulin pattern, beta-globulin pattern, fibrinogen pattern and gamma-globulin pattern were found in all eighteen cases. 3. All eighteen cases were divided into normal periodontal tissue group, dental granuloma group, and radicular cyst group by the histopathologic diagnosis. The electrophoretic pattern of dental granuloma group and that of normal periodontal tissue group resembled each other. The two groups showed the highest percentage in beta-globulin fraction, and the beta-globulin of dental granuloma group(47.17%) was higher than that of normal periodontal tissue group (40.54%) by 6.63%. On the contrary, beta-globulin fraction of radicular cyst group (28.00%) was much lower than those of the granuloma group (47.17%) and normal periodontal tissue group (40.54%), and alpha-globulin of radicular cyst group (34.16%) was much higher than those of the granuloma group (20.04%) and normal group (19.58%). 4. Five cases (31.3%) of the sixteen periodontal lesions showed different results between histopathologic diagnoses and radiographic findings.

• Journal of the Korean Society of Food Science and Nutrition
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• v.5 no.1
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• pp.25-30
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• 1976

In this investigation, the physico-chemical properties of Korean cattles milk and Holstein cows milk are studied. The results of the milk -protein of F-1, F-2, and F-4 hybrid are interested in this studied. 1. The physico-chemical properties of Korean cattle and Holstein cows milk is summarized at Table 1, Table 2. 2. The electrophoretic milk protein fraction of Korean cattle is identified : Lactoalbumin 1.74mg%. Alpha-1 globulin 1.19mg%, Alpha-2 globulin 0.68mg%, Beta-globulin 2.57mg%, Gamma-globulin 0.93mg%. 3. The electrophoretic milk protein fraction of Holstein cow : Lactoalbumin 1.23mg%, Alpha-1 globulin 0.93mg%, Alpha-2 globulin 0.86mg%, Bata-globulin 2.56mg%, Gamma-globulin 1.74mg% have been identified. 4. The electrophoretic milk protein fraction of hybrid F-1, F-2, and F-4 between Korean cattle(female) and Holstein(male) is obtained the following : F-1 hybrid : Lactoalbumin 1.38mg%, Alpha-1 globulin 1.58mg%, Alpa-2 globulin 2.46mg%, Beta-globulin 1.39mg%. F-2 hybrid : Lactoalbumin 1.57mg%, Alpha-1 globulin 1.74mg%, Alpha-2 globulin 2.19mg%, Beta-globulin 1.74mg%. F-4 hybrid : Lactoalbumin 2.46mg%, Alpha-1 globulin 1. 24mg%, Alpha-2 globulin 1.57㎎%, Beta-globulin 1.74mg%.

• Korean Journal of Clinical Laboratory Science
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• v.38 no.2
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• pp.111-116
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• 2006

One of the cardinal findings of the renal diseases is proteinuria, which appears in the early phase of kidney diseases and is very important in diagnosis, prognosis and decision making in the treatment process and results of the treatment. The study subjects were 126 patients who visited the nephrology department of Kangbuk Samsung Hospital. Serum was requested for urine protein electrophoresis. Total protein was measured with Bayer Advia 1650 (Biuret). Quantitation of each fraction was done by multiplying the percentage of each fraction by the total protein. Serum creatinine and BUN were also measured with Bayer Advia 1650 (Jaffe and Urease). Serum protein EP was done with REP(rapid electrophoresis) using Helena Kit reagents (REP Ultra SPE Kit, Ponceau S stain, Acetic acid, Methanol, EP Control). Concentrated urine was used for urine protein EP. The SPSS package was used for statistics analysis. Percentage and quantitation of the level of albumin in renal diseases were significantly lower than those in healthy controls. Total protein was correlated with albumin. In terms of proportion, ${\alpha}1$-globulin, ${\alpha}2$-globulin, ${\beta}$-globulin, and ${\gamma}$-globulin fractions were increased in the disease group. But, in the quantified level, ${\alpha}2$-globulin was increased and ${\beta}$-globulin and ${\gamma}$-globulin were decreased. ESRD patients showed an increased secretion of high molecular proteins in urine protein EP. A decreased level in serum total protein correlated with the decreased level of serum albumin and the total amount of urine total protein. This study revealed the variety in the level of serum and urine proteins and their subgroups by EP.

• Korean Journal of Veterinary Research
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• v.37 no.2
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• pp.451-456
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• 1997

120 heads of korean native calves were examined of serum protein by using cellulose acetate electrophoresis. During 20 days since the calves were purchased, serum protein, fibrinogen values and plasma : fibrinogen ratio were examined in the calves with respiratory and diarrheal disease. The result obtained in this investigation were as follows : 1. Among the 120 heads of calves that were purchased from market, 14 heads(22%) of calves were occurred respiratory disease, and 12 heads(20%) of calves are occurred diarrhea. Occurrence of respiratory disease was 14.5(4~20) days in average and diarrhea was 9.6(2-15) days after they had been purchased. 2. Serum protein fraction were analyzed by cellulose acetate electrophoresis. ${\beta}-globulin$, A/G ratio and ${\beta}_2-globulin$ values were decreased in the calves with respiratory disease. Especially, ${\beta}_2-globulin$ were significantly decreased. In calves with diarrhea, there was no change in ${\beta}-globulin$ values. ${\beta}_2-globulin$ values were higher than that of the normal and respiratory diseased calves. 3. ${\alpha}-globulin$ values were increased in both of calves with diarrhea and respiratory disease. This tendency was due to increase ${\alpha}_2-globulin$ values. 4. The $\gamma$-globulin value of calves with diarrhea was the lowest among the 3 groups. 5. The total protein values of normal calves were $7.0{\pm}1.1g/dl$ and that of respiratory and diarrheal diseased calves were $6.9{\pm}0.9g/dl$ and $6.6{\pm}0.8g/dl$, respectively. Total protein value of calves with diarrhea was lower than that of normal and respiratory diseased calves. Globulin value of calves with diarrhea was the lowest among them. The low value of total protein in diarrheal diseased calves was due to decrease globulin values. 6. The fibrinogen values of calves with respiratory disease ($643{\pm}189mg/dl$) were significantly higher than that of normal calves($533{\pm}135mg/dl$) and calves with diarrhea($572{\pm}188mg/dl$). The plasma : fib. ratio of respiratory diseased calves was $12.0{\pm}4.9$, normal calves was $13.8{\pm}3.5$ and diarrheal diseased calves was $12.8{\pm}4.6$. The ratio of the calves with respiratory disease was significantly decreased.

• Applied Biological Chemistry
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• v.20 no.1
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• pp.26-32
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• 1977

The multiple 7S globulins composed of two fractions (A and B) in the electrophoresis with Davis' method were isolated at different stages of the soybean seed development. Electrophoresis of their subunits liberated in PAWU solvent [phenol-acetic acid-water (2 : 1 : 1) solution plus 5M urea] yielded 4 major bands. Observation of both the electrophoretic bands of the multiple 7S fractions(7S-A and 7S-B) and those of their subunits was suggestive of a similarity of the subunit pattern between two 7S fractions. The two fractions in multiple 7S globulins were isolated with DEAE-Sephadex A-50 column$(2.0{\sim}100cm)$ chromatography. They were separated into 2 fractions in a linear gradient concentration of 0.28 to 0.40M NaCl with phosphate buffer (pH 7.8) containing 10mM ${\beta}-mercaptoethanol$(ME). The isolated protein was dissociated into subunits with two different solvent systems; in PAWU solvent and in Tris-HCl buffer(pH 8.0) containing 1% sodium dodecyl sulfate (SDS) and 40mM ME. The dissociated subunits were subjected to electrophoresis in PAWU-treated 7.5% acrylamide gel and in 1% SDS-treated 5.6% acrylamide gel. In PAWU gel electrophoresis, total 7S globulin was separated into 5 major bands, two of which were occupied in common by two 7S fractions(7S-A and 7S-B). In SDS gel electrophoresis, total 7S globulin was separated into 7 major bands, three of which were overlapped with the subunit of the two 7S fractions. The above results alluded us to the presence of a common and/or similar subunit between the multiple 7S globulins.