• The Korean Journal of Zoology
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• v.34 no.2
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• pp.159-172
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• 1991

It has been investigated what could be the selective marker distinguishing the immature from mature spermatozoa and whether fi -glucuronidase and fi -glucosidase are dependent on androgen in the luminal fluid of the epididymis or not. The contents of hexose, hexosamine and sialic acid in the epithelial cells, luminal fluid and spermatozoa of the epididymis were examined and the patterns of protein bands were compared in each group of the luminal fluid by SDS-PAGE. Lactate dehydrogenase, glucose-6-phosphatase, Na+ -K+ -ATPase and MgNa-ATPase showed higher activities in the cauda than the caput epididymal spermatozoa but only $Mg^2$+-ATPase activity appeared to be changed significantly. When the contents of hexose, hexosamine and sialic acid were analyzed and compared quantitatively, those of hexose were significantly different in the luminal fluid of caput and cauda epididymis, those of hexosamine in the epithelial cells and those of sialic acid in the epithelial cells and luminal fluid. When SDS-PAGE has been performed in each group, the band of MW 33-37 KD which was absent in the luminal fluid of caput epididymis appeared obviously in the luminal fluid of cauda epididymis and ako apeared in the cauda sperm crude membrane fraction. In addition, $\beta$ -glucuronidase and $\beta$ -glucosidase activities and their dependence on androgen were measured and the SDS-PAGE patiems of proteins and/or glycoproteins in the luminal fluid were examined. The activities of these two enzymes in the luminal fluid of the epididymis decreased significantly from the 5th day after castration. When testosterone was injected, the activity of $\beta$ -glucuronidase began to increase significantly from the 5th day following injection and that of $\beta$ -glucosidase from the loth day. On the other hand, the band of about MW 21 KD was newly observed in the lumen of caput epididymis when testosterone was administered.

• Parasites, Hosts and Diseases
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• v.26 no.2
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• pp.87-94
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• 1988

By affinity chromatography using a monoclonal antibody as ligand, Kim et at. (1986) purified a protein fraction in cystic fluid of Taenia solium metacestodes (CF) In this study, the biochemical properties of the purified protein were characterized. Discontinuous-polyacrylamide gel electrophoresis (disc-PAGE) of the protein at 4.5∼10% separating gel concentration showed its molecular weight (MW) to be 150 kilodalton (kDa) in non·denatured state, while denaturing sodium dodecyl suifate-polyacrylamide gel electrophoresis (SDS-PAGE) revealed that it was composed of 3 different subunits with respective fnw of 15, 10 and 7 kDa. Subunit of 7 kDa was shown to be linked to other subunits by disulade bonds. Isoelectric point of the protein was pH 6.8. The protein was relatively heat-stable for immunologic analysis. These properties indicated that the protein, comprising about 70% of total content in CF, had similar biochemical characters with antigen B of Oriol et at.(1971) in hydatid cyst quid (HF).

• Korean Journal of Food Science and Technology
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• v.25 no.1
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• pp.39-45
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• 1993

The effects of enzymatic modification with pepsin and actinidin was studied on molecular weight distributions and functional properties of hydrolysates from soy protein isolate (SPI) differing in degree of hydrolysis. The hydrolyzed SPI by pepsin showed 41.5% degree of hydrolysis after 5 min, and maximum hydrolysis was obtained after 2 hours. Actinidin hydrolyzed SPI 26.71% degree after 1 hour. On SDS-PAGE, native SPI showed 9 distinguishable bands on SDS-PAGE gel. Pepsin treated SPI showed one broad band in the lower part of gel. This band was shifted further to the bottom of the gel and became faint as hydrolysis time increased. While actinidin treated SPI showed different SDS-PAGE pattern from pepsin. However PAGE patterns were similar with pepsin and actinidin treated groups. With pepsin treatment, solubility of SPI distinctively increased around isoelectric point(pI). Emulsifying activity (EA) and emulsifying stability (ES) showed marked increase over pH range of $3.0{\sim}8.0$. 5 min modified group had most excellent foam expansion (FE). Foam stability (FS) was increased as pepsin treatment time increased at pI. With actinidin treatment, solubility was increased. 60 min modified SPI had the most effective EA at pH 4.5. However ES was not effected by actinidin treatment. 5 min modified group was most effect in FE. FS was higher at alkaline pH.

• Korean Journal of Microbiology
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• v.38 no.2
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• pp.67-73
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• 2002

The cellular responses of soil-borne bacterium, Pseudomonas sp. HK-6 to explosive 2,4,6-trinitrotoluene (TNT) were examined. Two stress shock proteins (SSPs), approximately 70-kDa DnaK and a 60-kDa GroEL were found in HK-6 cells in response to TNT. Analyses of SDS-PAGE and Western blot using anti-DnaK and GroEL revealed that SSPs were induced in HK-6 cells exposed to 0.5 M of TNT far 6-12 hrs. The maximum induction of proteins was achieved at 8-hr incubation point after HK-6 cells'exposure to TNT. Similar SSPs were found to be induced in HK-6 cells by heat shock (shift of temperature, from $30^{\circ}C$ to $42^{\circ}C$) or cold shock (shift of temperature,$30^{\circ}C$ to $4^{\circ}C$).2D-PAGE of soluble protein tractions from the culture of Pseudomonas sp. HX-6 exposed to TNT demonstrated that approximately 450 spots were observed on the silver stained gels ranging from pH 3 to pH 10. Among them, 12 spots significantly induced and expressed in response to TNT were selected and analyzed. Approximately 60-kDa protein, which was assumed highly expressed on the gel, was used for amino acid sequencing. N-terminal microsequencing with in-gel digestion showed that N-terminal sequence of the TNT-induced protein, <$^1XXAKDVKFGDSARKKML^17$, shared extensive similarity with $^1XXAKDVKFGDSARKKML^17$, N-terminal sequence of (P48216) GroEL of Pseudomonas putida.

• Korean Journal of Veterinary Research
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• v.32 no.2
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• pp.195-205
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• 1992

The soluble antigen profiles and antigenic specificities of Leptospira interrogans serovars icterhaemorrhagiae, canicola, pomona and hardjo were examined by SDS-polyacrylamide gel electrophoresis, crossed immunoeletrophoresis and immunoblotting. The profiles of protein, glycoprotein and fraction containing N-acetylglucosamine of 4 serovars were compared. The protein profiles of 4 serovars were very similar except the range of 14,400 to 30,000 daltons. Molecular weight of glycoprotein of L, pomona was lower than other serovars. L canicola showed extra N-acetylglucosamine bands having molecular weight of 82,000 and 90,000 daltons. In crossed immunoelectrophoresis, a close antigenic relationship was found between L icterohaemorrhagiae and L canicola. In immunoblottings conducted with soluble antigens and rabbit antisera of 4 serovars, Leptospira interrogans serovars possessed cross-reactive antigens and serovar-specific antigens. The molecular weights of serovar-specific antigens were 45,000, 82,000 and 90,000, 31,000 and 24,000 daltons in L icterohaemorrhagiae, L canicola, L pomona, and L hardjo, respectively.

• Korean Journal of Microbiology
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• v.30 no.6
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• pp.501-506
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• 1992

An alkalophilic Vibrio sp. RH530 showing high proteolytic activity was isolated form soil samples by enrichment culture. The activity staining using gelatin SDS- polyacrylamide gel electrophoresis (PAGE ) revealed that the strain produced an alkaline major protease (Apr B) with a size of 27 kDa, and at least six minor proteases. The apparent sizes of four of the minor proteases were approximately 45, 28, 22 and 19 kDa. Apr B and five of the minor proteases were inhibited by serine protease inhibitors including PMSF and DFP, suggesting that they are serine proteases. One of the minor proteases was inhibited by metalloprotease inhibitors, not by serine protease inhibitors, indicating it to be a metalloprotease. Furthermore, the activities of Apr B and Prt 3 were not inhibited by SDS in the reaction mixture. The production of Apr B and some of the minor proteases was specifically affected by culture temperature (30 to 37.deg.C) and pH (7 to 10). The production of Apr B. Prt 2, Prt 5 and Prt 6 was mainly affected by culture temperature, while Prt 4 by culture pH. Prt 1 and Prt 3 were not affected by neither of these factors.

• Journal of the Korea Academia-Industrial cooperation Society
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• v.13 no.1
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• pp.439-444
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• 2012

This study was conducted to determine the effects of electrolytic water washing(EWW) and tap water washing(TWW) on proximate composition, color difference and SDS-PAGE changes of Mackerel(Scomber japonicus) muscle. Moisture contents of washed mackerel sediments EWW were much higher than TWW(p<0.05). Crude proteins of washed mackerel sediments EWW were 1% lower than TWW. Crude lipides had same results with crude proteins. Hunter value L, a, b were tested to each samples. $L^*$ values of TWW were higher than EWW. Both of $aL^*$ values were lower with washing times in order of 3rd>2nd>1st(p<0.05) but 2nd and 3rd of EWW were not significantly different(p>0.05). $b^*$ values were not different between the TWW and EWW(p<0.05). SDS-PAGE patterns of EWW muscle sediments were more darkeness 205KD band than TWW muscle sediments. In these results said that EWW is better than TWW for red meat kamaboko industry, respectively.

• Food Science of Animal Resources
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• v.23 no.2
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• pp.155-160
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• 2003

The purpose of this study was to purify epidermal growth factor(EGF) as growth factor from human colostrum. The effects of purified EGF fraction were directly related to the growth of cells. Results were as follows; After eliminated fat from colostrum, skim milk was obtained. We obtained the EGF fraction by performing ultrafiltration and gel filtration, and then were convicted by SDS-PAGE. The result of analysis of purified EGF fraction by high performance liquid chromatography(HPLC) was shown a peak at 31.185 min period. And it was similar with standard EGF that was shown a peak at 31.545 min. 10 ng of EGF was contained in 10 mg/mL through immunoassay to measure EGF content from isolated fraction. After SDS-PAGE, isolation degree of purified fraction was convicted through western blotting. BALB/3T3 cell was the most effectively stimulated and proliferated at 1 mg/mL concentration of the purified EGF fraction and percentage of cell proliferation was about 95%. In the case of IEC-6 cell, that was about 71%.

• Korean journal of applied entomology
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• v.27 no.4
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• pp.211-218
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• 1988

Polyhedral proteins and the endogenous alkaline protease associated with larval-derived polyhedra of nuclear viruses isolated from Spodoptera litura, Bombyx mori, and Hyphantria cunea were investigated. Polyhedral proteins prepared under alkaline protease heat-inactivated condition were separated as one band with 31Kd in S. litura a H. cunea NpV and 30Kd in B. mori NPV by the SDS-polyacrylamide gel electroptoresis. Whereas polyhedral proteins without heat-inactivation were degraded into smaller polypeptides with a certain pattern in alkaline solution. The results of double-immunodiffusion and western blot analysis with antisera against polyhedral proteins indicated that those three polyhedral proteins had common antigenic determinants and the degradation of polyhedral proteins by alkaline protease could be confirmed.

• Applied Biological Chemistry
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• v.30 no.2
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• pp.163-168
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• 1987

A method, based upon the separation of cellular proteins by one-and two-dimensional electrophoresis was used for distinguishing butween Bradyrhizobium japonicum strains and Rhizobium fredii strains. Significant differences in protein pattern of one-dimensional SDS-PAGE vs-ere observed between Rhizobium fredii strains and Bradyrhizobium japonicum strains. The differences in six distinct main lands were observed among total 52 kinds of protein bands. Furthermore, the distribution of proteins in two groups by two-dimensional polyacrylamide gel electrophoresis was very different. The majority of visible proteins of Rhizobium fredii were acidic, whereas those of Bradyrhizobium japonicum were basic. In addition, amino acid composition was analyzed to detect the differences between two groups. No significant differences in amino acid composition were observed between Bradyrhizobium japonicum strains and Rhizobium fredii strains. The results indicate that one-and two-dimensional polyacrylamide gel electrophoresis were useful for identifying rhizobia isolates. One-dimensional SDS-PAGE of rhizobia proteins provided a rapid method for screening a large number of isolates, whereas two-dimensional electrophoresis was more of resolution and easiness for analyzing protein spots.