• Applied Biological Chemistry
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• v.31 no.4
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• pp.361-370
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• 1988

To investigate the interaction between whey and soybean protein, thermal changes of component proteins were analyzed by column chromatography and gel electrophoresis. In the Sephadex G-200 chromatography of the mixture treated at above $80^{\circ}C$, the amount of low molecular weight proteins and high molecular aggregates were increased. This implicated that dissociation of 1ls globulin into subunits and the formation of soluble aggregates between these subunits and whey proteins that contain thiol and disulfide groups. These interaction between soy proteins and ${\beta}-lactoglobulin$, ${\alpha}-lactalbumin$, and proteose-peptone 3 were confirmed by gel electrophoresis. Bovine serum albumin, Immunoglobulin-G(H), Lactoferrin, 1ls-subunits(basic and acidic), and subunit of 7s globulin were also considered to interact each other depending on the condition of the salt solutions.

• Korean Journal of Food Science and Technology
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• v.10 no.4
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• pp.415-422
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• 1978

Some minor Korean beans including red bean, mung bean and kidney bean were subjected to proximate analysis, fractionation by the solubility method and polyacrylamide gel disc electrophoresis of proteins to obtain the following results. 1) Proximate composition of the beans showed that fat content was less than 1%, carbohydrate was about 60% and protein content was in the range of $20{\sim}25%$. 2) Total globulin content of the proteins was $46{\sim}59%$, a little lower than in soybean, in the order of mung bean> kidney bean> red bean. Albumin content was comparable in kidney bean, and lower in red bean and mung bean as compared with that in soybean. Glutelin content was relatively higher, being in the range of $10{\sim}19%$ and in the order of red bean> mung bean> kidney bean. 3) According to the electrophoretic pattern, total protein fractions extracted with pH 7.6 buffer from red bean, mung bean and kidney bean showed 9.12 and 11 bands, respectively, whereas those extracted with pH 4.8 buffer showed 13, 13 and 12 bands, respectively. Water extracts of red bean, mung bean and kidney bean showed 10, 8 and 9 bands, respectively, while albumin fractions showed 8, 9 and 7 bands and globulin fractions, 4 bands in all of three beans. The band having a Rm value of $0.5{\sim}0.7$ in the globulin fraction from three beans was not observed in the water extract and appears to be specific to water insoluble globulin.

• Applied Biological Chemistry
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• v.10
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• pp.15-21
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• 1968

In order to fractionate the rice protein employing paper electrophoresis, 9 subjects of Korean rice and one Indica type, Pin Galw 50 were examined, the results were as follows. 1. Polished rice protein was separated into albumin, globulin, prolamine, and oryzenin. The amount of these fractions was determined by Kjeldahl method showing respectively 0.26%, 0.65%, 0.41%, and 5.01% in average. Albumin was extracted with deionized water, globulin with 10% NaCl, prolamine with 70% ethanol, and oryzenin with 0.05N-NaOH. 2. Albumin was extracted with deionized water and dialyzed by a cellophan tube. The supernatant was submitted to paper electrophoresis using phosphate buffer (pH 7.6, ${\mu}$ 0.18). Albumin was identified as monocomponent in all of 10 varieties under study. Globulin was extracted and dialyzed to remove the albumin. The precipitates were resolved in 10% saline solution and examined by paper electrophoresis. The globulin consists of two components in phosphate buffer(pH 7.6, ${\mu}$ 0.18) Any subject, regardless the origin, appears to contain globulin I and globulin II. Prolamine was extracted with 70% ethanol, dialayzed against deionized water, resolved with ethanol, and analyzed by Paper electrophoresis. It was proved as one component in the 70% alcoholic buffer(pH 9.0, ${\mu}$=0.0095). On the contrary, paper electrophoresis with oryzenin demonstrated two or three components in Sorensen's buffer(pH 13.0, ${\mu}$ 0.11). Yookoo 132, Dungpan 5, Kwansan, and Jaekun contain oryzenin I, oryzenin II, and oryzenin III. On the other hand, Paldal, Jinheung, Sukwang, Eunbangzu, Damakum, and Pin Galw 56 contain only oryzenin II, and oryzenin III. On the basis of these analyses a discussion of the differences between the protein fractions of 10 varieties was presented. 3. Globulin I varied from 0.22% to 0.46% (aver. 0.35%) in the amount, globulin II from 0.21 to 0.44%(aver. 0.32%), oryzenin I from 0.17% to 0.44%(aver. 0.3%), oryzenin II from 1.59% to 2.88%(aver. 2.23%), and oryzenin III from 2.02% to 3.57%(aver. 2.66%).

• Current Research on Agriculture and Life Sciences
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• v.3
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• pp.151-157
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• 1985

This study was carried (Jut to find out changes of ${\gamma}$-globulin and cholesterol of rat blood fed on yoghurt and Koumiss. Yoghrt and koumiss were manufactured with fortifed milk and Lactobacillus bulgaricus, streptococcus thermophilus and Saccharomyces fragilis were used. The twenty rats were devised into 4 groups with 5 replications by completely randomized design. The experimental groups are the control, milk, yoghrt and koumiss feeding groups. The results are summerized as follows ; The changes of pH after 8hrs incubation with Lactobacillus bulgricus, Streptococcus thermophilus and the mixed strains were 3.7, 4.6 and 3.5 at $42^{\circ}C$, respectively. Average alcohol percentage of Koumiss was 1.2 (%). The average viscosity of yoghurt and Koumiss with milk showed 1500 cp and 390 cp. respectively at 11 % of milk total solid. ${\gamma}$-globulin contents in blood of rat fed on yoghurt and Koumiss were higher than those of control and milk. Cholesterol of rat blood in yoghurt and Koumiss group were lower than those of control and milk group.

• Journal of Veterinary Science
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• v.23 no.6
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• pp.85.1-85.11
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• 2022

Background: Neonatal calf diarrhea is a major problem in the cattle industry worldwide. Rotavirus and Cryptosporidium parvum are the primary causative agents, especially during the first three weeks of the calf's life. Objectives: This study investigated the differences in acid-base, electrolytes, and biochemical parameters of diarrheic calves with infection of either rotavirus or C. parvum. Methods: A total of 61 Korean native calves (≤ 20 days old) were divided into two groups based on rotavirus or C. parvum infections: rotavirus infection (n = 44) and C. parvum infection (n = 17). The calves with at a specific blood pH range (pH 6.92-7.25) were chosen for comparison. The acid-base, electrolyte, chemistry, and serum proteins were analyzed, Further, fecal examinations were performed. Results: Compared to C. parvum-infected calves, the rotavirus-infected calves showed lower levels of total carbon dioxide, bicarbonate (HCO₃^-), anion gap, total protein, and albumin/globulin ratio, and significantly lower levels of potassium, globulin, and α2-globulin (p < 0.05). The C. parvum-infected calves (r = 0.749) had stronger correlations between pH and HCO₃^- than the rotavirus-infected calves (r = 0.598). Compared to rotavirus-infected calves, strong correlations between globulin and α2-globulin, α2-globulin and haptoglobin were identified in C. parvum-infected calves. Conclusions: This study is the first to investigate acid-base, electrolyte, and biochemical parameters in calves in response to infections of rotavirus and C. parvum. Although rotavirus and C. parvum cause malabsorptive and secretory diarrhea in similar-aged calves, blood parameters were different. This would help establish the diagnostic and treatment strategies.

• Journal of agriculture & life science
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• v.43 no.5
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• pp.39-42
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• 2009

Soybean is an important sources of plant proteins for human and animal nutrition. The use of soybean proteins has been expanded in the food industry due to their excellent nutritional benefits. But, Soybeans contain allergenic proteins that cause allergies to sensitive individuals. ${\beta}$-conglycinin(7S globulin) and glycinin(11S globulin) are the major components of storage protein in soybean. ${\beta}$-conglycinin consists of three subunits, ${\alpha}^{\prime}$, ${\alpha}$, ${\beta}$ and exhibits poorer nutritional and food processing properties than glycinin. There is a great deal of interest in the development of soybean lines with reduced amounts of ${\beta}$-conglycinin. The objective of this study was to determine the inheritance of ${\alpha}^{\prime}$-subunit protein in 7S globulin. F2 population was developed from the cross of "Jinpumkong2ho"(${\alpha}^{\prime}$-subunit presence) and PI506876(${\alpha}^{\prime}$-subunit absence) parent. Total 98 of F2 seeds were obtained and analyzed for the segregation of ${\alpha}^{\prime}$-subunit protein by SDS-PAGE. Among 98 F2 seeds, 70 F2 seeds showed ${\alpha}^{\prime}$-subunit protein and 28 F2 seeds did not show ${\alpha}^{\prime}$-subunit protein. The segregation ratios of 3 : 1 for presence and absence of ${\alpha}^{\prime}$-subunit protein were observed(${\chi}^2=0.667$, P=0.414). These data indicate that presence and absence of ${\alpha}^{\prime}$-subunit protein is controlled by a single major gene and might be useful for strain selection of 7S protein reduced soybean.

• Journal of the Korean Society of Food Science and Nutrition
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• v.25 no.5
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• pp.878-884
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• 1996

A bacterial strain, designated as Bacillu sp. IJ-3 strain, was shown to produce the extracellular soy protein coagulating enzyme and culture conditions for the production of enzyme by this microbial strain was investigated. The culture medium giving a maximum soy protein coagulating activity was consist of 20%(w/v) soymilk, 2.0%(w/v) glucose, 4.0%(w/v) yeast extract, 5.0%(w/v) polypeptone and 1.0%(w/v) potassium phosphate, monobasic. Initial pH was optimal at 6.0 and the enzyme activity in the culture usually reached a maximal level of fermentation at $35^{\circ}C.$ After the culture medium adjustment where required, enzyme activity was reached maximum at 72 hour of cultivation but this enzyme activity was reduced quickly. It can be assumed that Bacillu sp. IJ-3 strain enzyme has a specificity toward the 75 globulin.

• Parasites, Hosts and Diseases
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• v.28 no.2
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• pp.101-108
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• 1990

Surgically collected cystic fluid of Taenia solium metacestodes from patients of intracranial cystic lesion were compared in their protein composition with those from naturally infected pigs in Cheju Do, Korea and Ecuador. In non-denaturing discontinuous-polyacryla aide gel electrophoresis (disc-PAGE) , no discernible differences were recognized in banding patterns between the cystic fluids from Cheju Do and Ecuador, and between the cystic quids from pigs and human lesions except wider bands that corresponded to human albumin and T-globulin (in 4 of 9 patients). In reducing SDS-PAGE, bands in the cystic Ruid from Ecuador showed the same banding pattern with that from Cheju Do but two bands of 21 and 17 kDa were stained darker. Cystic quids (rom patients revealed the same protein compositions of the major protein bands of 94, 64, 15, 10 and 7 kDa as in the cystic fluid of pig origin, but human albumin (66 kDa), heavy and light chains of gamma globulin (55 and 22.5 kDa) were contaminated in 4 of 9 cystic fluids. Human CSF proteins seem to have been contaminated during cystic ftuid collection. In any cystic quid from patients, the majcr Protein component was 150 kDa which was subdivided into 15, 10 and 7 kDa in reducing SDS-PAGE.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.49 no.2
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• pp.141-147
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• 2004

This study was carried out to know the variation of soybean seed proteins, 11S and 7S globulins, and their amino acid compositions among different colored soybean varieties, 'Danbaegkong' (yellow), 'Pureunkong' (green) 'Jinyulkong' (brown), and 'Geoumjeongkong l' (black). Soybean seed proteins showed a wide range in molecular size, but the electrophoresis patterns of total seed protein subunits showed a similarity among different colored soybean varieties. Amino acid compositions of total seed proteins were similar for all soybean varieties tested. However, soybean varieties showed low composition rates in sulfur containing amino acids. The composition rates of cysteine and methionine in the 11S globulins were higher than those of total seed proteins and 7S globulins. Glutamic acid and glycine were higher in the 11S and 7S globulins than those of total seed proteins. However, the levels of methionine and phenylalanine are high in the 11S globulins, but those of valine and lysin are slightly lower than the 7S globulins. By using HPLC, we tried to analyse the soybean seed proteins. The 11S globulin was composed of 10 major peaks whereas the 7S globulin was composed of 4 major peaks. The composition rates of 11S related proteins have a tendency to increasing during the maturing whereas those of 7S related proteins have a tendency to decreasing. Composition rates of each peaks among different colored soybean varieties suggested that soybean seed proteins are varied, although they showed similarity in the electrophoresis patterns, and understanding of this characteristics is important for the utilization of soybeans.

• KSBB Journal
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• v.7 no.1
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• pp.39-44
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• 1992

Dose-dependent responses indicated by the increase of leukocyte, peritoneal exudate cell and weights of immunorgans revealed the improvement of immunity. In the effect of macrophage on phagocytes, there were not substantial differences in the phagocytic and corrected phagocytic index. The administered group being compared with the controlled group, there were no significant changes in SGOT, S-GPT, alaline phosphatase, total protein, albumin, globulin, cholesterol, triglyceride, blood urea nitrogen and glucose. Key words: dose-dependent responses, peritoneal exudate cell, phagocytic idex, corrected phagocytic index.