• Korean Journal of Poultry Science
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• v.26 no.3
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• pp.179-188
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• 1999

The present was undertaken to establish a model for the control of adipocytes differentiation by using antibody from egg yolk. The emulsion of membrane protein of 3T3L-1 cell membrane protein with the complete Freund's adjuvant was firstly immunized in layer. Second and third boosting were undertaken with two weeks intervals by injection of the emulsion of the same antigen with the incomplete Freund's adjuvant. After 4 week of the first immunization, eggs were collected and antibody (IgY) was purified from egg yolk. The purity of IgY was 60-98% determined by single radial immunodiffusion (SRID) methods. Titer value of the antibody showed high reactiviy for the preadipocytes membrane protein measured by ELISA. When the IgY was added in the test media containing either 2.5% porcine serum or 10% FBS(control), the differentiation of 3T3L-1 cells and Glycerol-3-phosphate dehydrogenase(GPDH) activities was significantly decreased compared to the control cells(p〈0.05). When mice were subcutaneously injected with IgY raised against membrane protein of 3T3L-1 cells for 3 weeks, adipose tissue mass around ovary was tended to be decreased in female mice compared to those of control mice. It is suggested that a potential for manipulating of lipid accumulation through decrease in 3T3L-1 cell differentiation and fat accumulation in female mice by IgY treatment.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.30 no.3
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• pp.473-479
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• 1997

The yolk protein of spotted flounder, Verasper variegatus was purified by precipitation wit cold distilled water, followed by Sepharose CL-6B column chromatography. The purified protein was identified as vitellin by Ouchterlony's immunodiffusion test and immunoelectrophoresis. The purified vitellin from ovarian crude extracts has same antigenic determinants with the female specific serum protein, vitellogenin. The molecular weight of purified vitellin was estimated about 550 kD by gel filfration. The vitellin was composed of three major subunits with molecular weight of about 108, 85 and 31 kD, and two minor subunits. The vitellin was identified by western blot analysis using anti-vitellin antibody.

• Asian-Australasian Journal of Animal Sciences
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• v.13 no.7
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• pp.986-990
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• 2000

The quality characteristics and proximate composition of the eggs of pheasant, chukar, quail, and guinea fowl were compared. Eggs of the 4 species had a similar ovalish conical shape with blunt and pointed ends, showing the shape indices of 77.30-79.63 with no statistical difference. Egg weight was heaviest in guinea fowl (46.65 g), followed by pheasant (25.79 g), chukar (19.16 g) and quail (10.34 g). Proportion of yolk to the total egg weight was highest in pheasant (35.7%), followed by chukar (33.9%), quail (31.4%) and guinea fowl (30.6%). Albumen content was highest in quail showing 61.2%, while pheasant, chukar and guinea fowl were in the range of 55.6~57.4%. The ratio of yolk to albumen (Y/A) was highest in pheasant (0.65), followed by chukar (0.60), guinea fowl (0.55) and quail (0.52). The portion of shell to the total egg weight was highest in guinea fowl (13.5%) and lowest in quail (7.3%). The shell thickness of the eggs was thickest in guinea fowl ($462.8{{\mu}m}$), followed by pheasant ($241.5{{\mu}m}$), chukar ($231.8{{\mu}m}$) and quail ($174.8{{\mu}m}$). The contents of moisture, crude protein, crude fat and crude ash of whole egg were in the ranges of 74.26-74.50%, 11.98-12.77%, 10.83-11.91% and 1.02-1.10%, respectively, with no statistical difference (p>0.05) among the species. Albumen was high in moisture (87.46-87.99%) and very low in crude fat (0.09-0.13%), which was quite different from yolk. Yolk showed relatively low level of moisture (49.71-50.42%) and high levels of fat (31.48-32.32%), crude protein (15.12-15.99%) and crude ash (1.53-1.86%). No species difference in the proximate compositions of albumen and yolk was found except in crude ash content of albumen.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.25 no.5
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• pp.432-442
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• 1992

To identify the histological site of synthesis of yolk protein precursor, vitellogenin, by immunocytochemical method in the freshwater crab Eriocheir japonicus, we purified the yolk protein, vitellin, from crude egg extracts, and prepared the anti-rabbit serum against vitellin. Then, the site of vitellogenin synthesis was demonstrated by immunotytochemical method with PAP(peroxidase-antiperoxidase) reaction using the rabbit antiserum aganist vitellin. Female specific serum protein was identified in female serum by immunoelectrophoresis and Ouchterlony's immunodiffusion test for mature male and female sera. Based on the immunoelectrophoresis and Ouchterlony's diffusion test for mature male and female sera and crude egg extracts using antiserum against vitellogenic female serum absorbed with male serum, the female specific serum protein was identified as vitellogenin, detected in female serum only. The major yolk protein, vitellin, was purified from the crude egg extracts by DEAE-cellulose ion exchange chromatography, followed by sepharose CL-4B gel filteration chromatography. The molecular weight of vitellin was estimated to be about 245,000 dalton by sepharose CL-4B gel filteration chromatography. from the results of immunological analysis for vitellin, it was found that the vitellin antiserum contained the antibody against vitellogenin. In the results of immunocytochemical reaction by PAP method with the rabbit antiserum against vitellin, the vitellogenic oocytes and the hepatopancreas of mature female showed positive PAP reaction, but not in follicle cells and previtellogenic oocytes nf ovary, muscle of female and mature male hepatopancreas. Therefore, it showed that the hepatopancreas of mature female is the site of vitellogenic synthesis.

• Journal of Life Science
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• v.15 no.1 s.68
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• pp.9-14
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• 2005

Batch enzymatic hydrolysis of egg yolk protein by protease was carried out at laboratory scale coupled to an ultrafiltration module. Effect of ethanol concentrations on the performance of enzymatic hydrolysis was studied to determine the optimum condition of recovery of hydrolysate. The enzymatic hydrolysis was conducted stepwise with following conditions, $50^{\circ}C$, pH 10.0 and pH 6.5. Ethanol concentration was changed from 10 to $40\%$ (w/w). As ethanol concentration was increased, the recovery yield of total solid and protein in enzymatic hydrolysate was also increased. The content of sialic acid and protein in hydrolysate was independent of ethanol concentration. We also investigated the effect of ethanol concentration on the performance of ultrafiltration. As the concentration of ethanol in yolk protein was increased, the recovery yield of product was increased. Ultra­filtration of egg yolk protein hydrolysate was conducted to increase the content of sialic acid. Four ultrafiltation modules were used in this study, and we evaluated the performance of the UF modules. When Amicon module was used, the recovery percentage of total solid in retentate was $6.0\%$, which is the highest among the modules used. In spite of the difference in the recovery yield of total solid, the purity of sialic acid in retentate was about $2.0\%$, which was 5 times higher than that in feed. It was concluded that the recovery yield and the purity of sialic acid did not correlate with the types of modules and the size of MWCO.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.28 no.6
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• pp.753-760
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• 1995

This study was conducted to determine the serum vitellogenin (VTG) concentration changes during the ovulation period in elkhorn sculpin, Alcichthys alcicornis. The results of sepacryl S-300 showed that the molecular weight of VTG could be 380,000. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) analysis may indicate that the purified VTG consists of three subunits with molecular weights of 180,000, 118,000 and 85,000, respectively. Yolk protein purified from the egg extracts was eluted on an equilibrated sephacryl S-300 column, and its molecular weight was estimated 250,000. The precipitation lines of the female serum against the antiserum of the egg extracts were fused completely by immunoelectrophoresis and immunodiffusion analysis. VTG was detected in the serum, and hepatocytes from males injected with $17\beta-estradiol\;(E_2).$ Furthermore, VTG was immunochemically similar to yolk proteins. The concentration of VTG was high before ovulation $(9.80\pm0.81-11.02\pm0.09 mg/ml),$ and then decreased rapidly after ovulation $(less\;than\;6.19\pm0.59 mg/ml).$ This study suggested that VTG was synthesized in the liver by the action of $E_2$ and released to blood, and then incorporated into oocytes.

• Korean journal of applied entomology
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• v.34 no.2
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• pp.140-146
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• 1995

Changes in protein content during oocyte development was measured and egg-specific protein was characterized from the eggs in Lucilia illustris. During normal development ovarian protein was rapidly increased at 72hr and reached maximum at 96hr after a protein meal, when the eggs were fully matured. Purified protein from the ovaries by gel filtration of DEAE-cellulose an Sephacryl S-200 was loaded on 7.5% native polyacrylamide gel electrophoresis and identified at ${R}_{f}$ 0.4 as egg-specific protein, which has a mol. wt of 110,000. A total of 13 amino acids in th egg-specific protein was identified and expecially asparagine, glutamic acid, and tyrosine were highly concentrated. Five fatty acids were also identified. It is suggested that there is a specific protein in the eggs of L. illustris except yolk protein synthesized and secreted by fat body.

• Korean Chemical Engineering Research
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• v.49 no.6
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• pp.798-803
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• 2011

IgY(Immunoglobulin Yolk) is a specific antibody in egg yolk, and it protects human body from virus and antigen. There are a lot of egg yolk components such as lipoprotein and protein. To separate IgY, HPLC(High Performance Liquid Chromatography) and precipitation were used in a batch mode and SMB(Simulated Moving Bed) was adopted for continuous purification of yolk proteins. IgY and other proteins in yolk were separated by using three-zone SMB chromatography. Before performing SMB experiments, batch chromatography and PIM(pulse input method) were performed to find operation parameters and adsorption isotherms. The results of batch chromatography were compared with simulated results using Aspen chromatography. To find the most suitable separation condition in SMB chromatography, simulations in $m_2$-$m_3$ plane on the triangle theory were carried out. $m_2$ = 0.18, $m_3$ = 1.0 and ${\Delta}$t = 419 s are the best conditions for the highest purity of IgY. With this operating parameters(flow rate in three zone and switching time), the purity of raffinate results in 98.39% from Aspen chromatography simulation. Most of the simulation reached steadystate within second recycle.

• The Korean Journal of Zoology
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• v.32 no.4
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• pp.337-350
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• 1989

In this study, we compared patterns of hemolvmph with ovarian proteins during the yolk formation of Gewis paludum by using SDS/polyacrylamide gel electrophoresis and he dimen-tlonal electrophoresis. In addition, we examined patterns of glycoprotein which were composed of yolk substances. The results were as follows: The protein patterns in ovary of the 5th instar without eggs were similar to those of adult after ovulation. Protein amounts of the ovaw without developing eggs were less than those of the ovaw containing oocvtes or matured eggs at the molecular weights range from 66, 000 to 110.000 daltons. No glvcoproteins were observed in ovaw without eggs. But the glvcoproteins were gradually increased according to development of eggs in the 5th instar. After the ovulated ovaw of adult, no glvcoprotein bands urere occurred as the bands of the ovary without eggs in the 5th instar. Also, amounts of hemolvmph protein between 66, 000 and 110, 000 in molecular weight were increased during yolk formation of the 5th instal. The results suggest that ovarian protein substances may originate from hemolpnph. In the 5th instar, the amounts of glycoprotein of developing eggs was gradually increased in the hemolymph. The band of M.W. 29, 500 was occurred in the hemolpnph of the 5th instar and adult without eggs. This protein mal be precursor of glvcoprotein in the high molecular weight area in the ovary of more developed eggs. The number of spots and the amounts of protein in ovary without eggs were less than those of ovary containing eggs by two dimensional elec-trophoresis. The protein bands between 45, 000 and 110, 000 almost appeared in acidic field of he dimensional gel. Especially, the band, M.W. 109, 000, uras separated 3 spots, a1, a2, and as. The band, M.W. 102, 000, has spots which designated b1, b2, b3, and b4. Besides, proteins below M.W. 24, 000 were occurred less spots in the basic field than those of acidic field. The mechanism of intracellular organs (= cell organells) uras related to the yolk protein synthesis of oocyte in the process of yolk protein formation of derris pcfudum.

• Journal of Sericultural and Entomological Science
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• v.28 no.2
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• pp.15-20
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• 1986

This study was carried out to investigate the elucidation of gene expression in embryo formation of the Kidney mutant, especially yolk proteins in unfertilized eggs and template activity of m-RNA extracted from them. The results were summarized as follow ; There was no recognized qualitative difference in yolk proteins of unferilized eggs between the Kidney mutant and normal. There was not any difference, between Kidney mutant and normal in the molecular species of m-RNA derived from maternal origin with the template activity in vitro.