• Korean Journal of Food Science and Technology
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• v.18 no.2
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• pp.163-167
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• 1986

During the germination of mungbean seeds, the changes of water contents, total and soluble proteins, and electrophoretic pattern of the soluble proteins were examined. The moisture content of a dry mungbean was 12.7%, which was greatly increased after the soaking. Along to the germination period, the moisture contentof the mungbean sprouts was gradually increased up to 90.7%. The contents of total and soluble proteins were sharply decreased after the soaking of the mungbean and decreased gradually during the germination. PAGE of the soluble proteins showed two broad bands and three sharp bands. During the germination, two broad bands were weadened but other bands were relatively stable. SDS-PAGE showed 19 discrete bands and during the germination, the most of the bands were thinned or disappeared. But some of the protein bands were stable until the end of germination.

• Parasites, Hosts and Diseases
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• v.30 no.3
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• pp.209-218
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• 1992

When cystic fluid of Taenia solium metacestodes (CF) was filtrated through Sephacryl S-300 Superfine, major proteins were in fractions III add IV Major protein in fraction III was Band C protein of 150 kDa and that in fraction IV was Band N protein (Choi et of., 1990). When CF was electrophoresed in 0.9% agarose gel and reacted with anti-CF rabbit serum (RACF), two main bands, a long outer and a short inner band, were precipitated, together with 8 minor bands. RACF reacted with fraction III forming the long outer band whereas RACF formed the short infer band with fraction IV in immunoelectrophoresis (IEP) The long outer precipitin band of CF fraction III was similar to antigen B in hydatid fluid (HF) of Oriol et at. (1971), while the short inner band of CF fraction IV was similar to HF antigen 5 of Caption et at. (1967) . When HF was reacted with RACF, the short inner band was immunoprecipitated without forming the long outer band. Common antigenicity between CF and HF seemed to exist in fraction IV rather than in fraction III of CF. Patient sera of neurocysticercosis reacted more frequently with fraction III than with fraction IV.

• Journal of Life Science
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• v.29 no.12
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• pp.1408-1414
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• 2019

Enzymes are widely used in industrial applications such as detergents, food, feed production, pharmaceuticals and medical applications and major contributors to clean industrial products and processes. To screen, identify, and characterize the enzymes the zymography techniques are routinely used. The zymography technique is a simple, sensitive, and quantifiable technique that is widely used to detect functional enzymes following electrophoretic separation in sodium dodecyl sulfate (SDS)-polyacrylamide gels. The method is a versatile two-stage technique involving protein separation by electrophoresis followed by the detection of enzyme activity in polyacrylamide gels under non-reducing conditions. It is based on SDS-polyacrylamide gel (PAG) copolymerization with substrates, which are degraded by the hydrolytic enzymes restored in enzyme reaction buffer after the electrophoretic separation. Any kind of biological sample can be applied and analyzed on zymography, including culture supernatants of microbes, plants extracts, blood, tissue culture fluids, enzymes in foods extracts and metaproteome. The advantage of zymography is that it is possible to directly detect the protein with activity on the electrophoretic gel as well as confirm the activity at the nanogram level. Thus, this zymography technology can be applied in various fields. However, these advantages are rather disadvantageous and can often lead to experimental errors. In this review, the advantages, disadvantages, and problem solving of zymography technique are described.

• The KIPS Transactions:PartB
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• v.17B no.1
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• pp.79-84
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• 2010

Matching spots between two sets of 2-dimensional electrophoresis can make it possible to find out the generation, extinction and change of proteins. Generally protein spots are separated by 2-dimensional electrophoresis. This process makes the position of the same protein spot a little different according to the status of the tissue or the experimental environment. Matching the spots shows that the relation of spots is non-uniform and non-linear transformation. However we can also find that the local relation preserves the topology. This study proposes a matching method motivated by the preservation of the topology. To compare the similarity of the topology, we compared the distance and the angle between neighbour spots. Experimental result shows that the proposed method is effective.

• Analytical Science and Technology
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• v.11 no.2
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• pp.96-104
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• 1998

A photodiode array multichannel detector system for capillary electrophoresis was developed. The photodiode array detector for capillary electrophoresis (CE-PDA) has 1024 photodetectors and can analyze sample by measuring UV/VIS absorption spectrum in 275~675 nm wavelength range. The CE-PDA instrument can get a spectrum in 30 ms during sample separation and can be programmed by a PC to control various experimental conditions required for sample analysis. The performance of the multichannel CE-PDA instrument was tested using L-ascorbic acid and alizarin yellow GG mixture. The reproducibility test of the CE-PDA system showed 5.6% RSD.

• Korean journal of applied entomology
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• v.37 no.1
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• pp.59-64
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• 1998

A juvenile hormone binding protein (JHBP) has been isolated from the whole body homogenate of Galleria rnellonella final instar larvae by gel filtration. The isolated protein is homogenous as judged by column chromatography and gel electrophoresis in the presence and absence of denaturing agent. The JHBP has a relative molecular weight of 32 k by denaturing gel electrophresis and 28 k by gel filtration. The protein exhibits a dissociation constant of 3.9 x M for JH 111.

• 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.

• The Korean Journal of Zoology
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• v.29 no.1
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• pp.70-74
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• 1986

Cytochrome oxidase activities have been compared from crude sumibitochondrial preparations of rat skeletal muscle tissues. Fast red (type $II_A$) preparation has highest cytochrome oxidase activity, slow red (type I) next, and fast white (type $II_B$) the lowest. Differences of electrophoretic mobilities have been detected by heme staining. Migration of heme band is in the order of slow red>fast red>fast white from fastest to slowest. Results of immunoelectrophoresis have substantiated the above finding.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
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• 2005.10a
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• pp.177-181
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• 2005

근원섬유 단백질에 카제인염을 첨가함으로써 유화안정성이나 보수력을 증진시킬 수 있으나 가제인염은 열에 안정성이 떨어지는 단점을 가지고 있다. TGase가 이러한 카제인염의 단점을 보완해주는지 알아보기 위해 열량분석기와 전기영동을 이용하여 단백질의 변화를 측정하였다. 열량분석기의 경우 근원섬유 단백질과 카제인 염 단백질의 상호교차결합을 TGase의 첨가유무에 따라 실시하였으며 그 결과 TGase의 첨가는 각 단백질 열량변화가 나타나는 온도를 변화시켰으며 배양시간을 증가할수록 각 단백질별 열량변화의 차이를 보였고 peak의 크기에도 차이를 보였다. 또한 전기영동의 경우 MFP, SC, MFP:SC의 1:1 혼합액을 각각을 TGase 첨가한 것과 하지 않은 것을 비교한 결과, TGase의 첨가는 고분자 polymer를 만들어줌으로써 두 단백질간의 상호작용에 촉매제로써 작용한다는 것을 확인하였다.

• The Korean Journal of Zoology
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• v.17 no.3
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• pp.127-130
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• 1974

The lactate dehydrogenase isozymes in tissues of eight fresh water fishes were examined by cellulose acetate electrophoresis. The electrophoretic distribution of the isozymes showed clearly species-specific pattern. Various subbands were found more frequently in these fishes than in mammals. The isozyme pattern of muscle seems to tend to be the same with that of brain in these fishes. The fish lactic dehydrogenase suggested in many cases to be consisted of nonrandomly selected hybrids.