• 한국응용과학기술학회지
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• 제4권2호
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• pp.43-48
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• 1987

Isoelectric point and surface tension of twelve of the alkylcarboxy betaines such as 2-(trimethylammonio) dodecanoate, 2-(trimethyammonio) tetradecanoate, 2-(trimethylammonio) hexadecanoate, (dimethyldodecylammonio)ethanoate, (dimethyltetradecylammonio)ethanoate, (dimethylhexadecylammonio) ehtanoate, 2-(dimethylododecylammonio) propanoate, 2-(dimethyltetradecylammonio)proopanoate, 2-(dimethylhexadecylammonio)propanoate, 2-(dimethyltetradecylammonio)-3-phenyl propanoate, 2-(dimethyltetradecylammonio)-3-phenyl propanoate are tested. From the measurement of the isoelectric point, it was found that the isoelectric point were leaned toward the alkaline zone for c-alkylarbrxybetaines, and toward the acidic zone for N-alkylcarboxybetaines. At the range of the carboxybetaine concentration $2\;{\times}\;10^{-2}{\sim}2\;{\times}\;10^{-5}$mole/l, the surface tension of the aqueous solution were decreased to 30-38 dyne/cm, showing the tendency that the ability of lowering the surafce tension was depending on the increase of carbon atom number in the lipophilic alkyl chain. The critical micelle concetration measured by the surface tension and concentration curves have been found at the range of $10^{-2}{\sim}10^{-5}$mole/l.

• 공업화학
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• 제23권6호
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• pp.521-528
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• 2012

본 연구에서는 에틸렌 옥사이드가 부가된 양쪽성 계면활성제에 대하여 기본적인 물성(임계 마이셀 농도, 표면장력, 계면장력, 접촉각, 점도, 계면활성제 시스템의 상거동 등)을 측정하였다. 또한 계면활성제 수용액에 대한 제타 전위 측정과 QCM 실험을 통하여 양쪽성 계면활성제가 양이온 계면활성제에서 비이온 계면활성제로 작용이 전환되는 등 전점을 결정하였다. 제타 전위 측정에 의하여 결정한 DE3-OSA82-AO, DE5-OSA82-AO 및 DE9-OSA82-AO 계면활성제 시스템의 등전점은 각각 6.97, 6.93 및 7.10이며, 이 결과는 QCM 측정 실험으로부터 결정한 각각의 등전점 6.97, 6.83 그리고 7.02의 값과 거의 일치하였다. 표면 마찰 시험기를 사용하여 계면활성제로 세정한 섬유의 평균 마찰계수 값을 측정한 결과, 계면활성제 수용액의 pH가 중성인 조건에서 섬유 유연 효과가 우수함을 확인하였다.

• BMB Reports
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• 제33권4호
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• pp.300-307
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• 2000

Two glycoproteins were purified and biochemically characterized from the lichen X. parietina. Both behaved as enzymes with arginase activity and haemaglutinins. Secreted arginase (SA) contained galactose and glucose in the saccharide moiety and an isoelectric point of 4.54. The algal binding-protein (ABP) had N-acetyl-glucosamine and glucose as glycosidic residues and an isoelectric point of 3.53. Both proteins had the same molecular mass (58.6 kDa) and the same qualitative amino acidic composition. The results allowed us to consider these glycoproteins as isolectins, which have significant physiological roles in the relationship between photobiont and mycobiont of symbiotic association.

• Journal of Life Science
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• 제9권1호
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• pp.35-39
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• 1999

Elecrophoreticl analysis of a 36 kDa protein was runned by SDS-PAGE, isoelectric focusing (IEF) and two dimensional electrophoresis pattern. Major 36 kDa and 25, 46, 48, 66 kDa protein were detected by Coomassie blue stain on SDS-PAGE. Major 36kDa protein was eluted for production of antiserum for serological analysis, IEF and two dimensional electrophoresis. Isoelectric point of 36kDa was aout pH 8.5. Two dimensional electrophoresis of eluted 36kDa showed one point on the gel. Anti-36 kDa serum made by newzilland rabbit for serological test. In ELISA, final titer of antibody was 100×{TEX}$2^5}${/TEX} : 1. Neutralize ability of serum was examined by slide agglutination test and colonization test in rat. Anti-36 kDa serum agglutinated whole cell of V. vulnificus were inhibited colonization on intestine in rat. Accordingly In this paper contain some electrophoretical analysis and serological test of a 36 kDa OMP of V. vulnificus.

• 대한화학회지
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• 제6권1호
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• pp.29-31
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• 1962

電壓條件 永動時間 및 支持電解質溶液의 pH가 Al ion의 paper electrophoresis에 미치는 影響을 closed horizontal type의 泳動裝置를 써서 Michaelis buffer soln.으로 飽和시킨 paper strip에서 實驗的으로 檢討하였다. 그 結果 Al ion에 가장 適合한 pH, 電壓 및 泳動時間을 決定하였으며 pH=2.38에서 Al ion의 mobility는 $(1.004{\pm}0.0020){\times}10^{-4}\;cm^2\;sec^{-1}\;volt^{-1},\;Al(NO_3)_3\;soln.$의 isoelectric point는 pH=3.23 임을 알았다.

• 한국세라믹학회지
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• 제33권1호
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• pp.110-118
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• 1996

• 한국수산과학회지
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• 제27권5호
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• pp.495-500
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• 1994

수산 가공품 제조 공정중 수세 과정중에 필연적으로 나오는 수용성 단백질이 다량 함유된 폐액에 대해 등전점이동응집처리를 행하여 대부분의 수용성 단백질을 회수하였다. 그래서, 본 회수단백질 구분에 대한 등전점응집처리과정중의 단백질 성상변화 관찰과 동시에 식품가공품의 부 또는 주 원료로서의 이용가능성 타진을 목적으로 냉동 명태 고기풀 대용으로 사용하여 어묵제조를 시도해 보았다. 그 결과, 등전점 응집처리과정중에 약 $50\%$정도 수용성 단백질의 고분자화가 일어나 어묵과 같은 탄력중시 제품에 주원료로서의 사용은 불가능하였다. 그러나, $30\%$까지 냉동 명태 고기풀에 대해 대체 첨가하여 어묵을 제조했을 때는 색차, 젤리강도 및 조직감 관찰을 통해 관찰된 결과로는 냉동 명태고기풀로만 만든 어묵에 비해서도 전혀 손색이 없는 제품을 만들 수 있음을 확인할 수 있었다.

• Korean Chemical Engineering Research
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• 제50권3호
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• pp.455-463
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• 2012

본 연구에서는 에틸렌 옥사이드와 프로필렌 옥사이드가 부가된 DEP-OSA82-AO 양쪽성 계면활성제에 대하여 계면활성제의 기본적인 물성(임계 마이셀 농도, 표면장력, 계면장력, 접촉각, 점도, 기포 안정성 등)을 측정하였다. 또한 계면활성제 수용액에 대한 제타전위 측정과 QCM (quartz crystal microbalance) 실험을 통하여 양쪽성 계면활성제가 양이온 계면활성제에서 비이온 계면활성제로 작용이 전환되는 등전점을 결정하였다. 제타전위 측정을 통하여 결정한 양쪽성 계면활성제의 등전점은 QCM 실험을 통하여 결정한 등전점 결과가 거의 일치하였으며, 표면 마찰 시험기를 사용하여 측정한 유연력 측정 결과와도 일치하는 경향을 나타내었다. 특히 DEP32-OSA82-AO와 DEP34-OSA82-AO 계면활성제의 경우, 산성 조건 혹은 중성 조건일 경우가 알칼리성 조건에 비하여 섬유 유연 효과가 큰 것을 확인하였는데, 이러한 결과는 등전점 보다 낮은 pH 산성 혹은 중성 조건에서 DEP32-OSA82-AO와 DEP34-OSA82-AO 계면활성제가 모두 양이온 계면활성제로 작용함으로써 세탁 후 린스 과정에서 유연제로서 효과적으로 작용할 수 있음을 의미한다.

• Archives of Pharmacal Research
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• 제12권2호
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• pp.79-87
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• 1989

Enzymatic methylation of arginine and lysine residues of several cytochrome c and lysine residue of calmodulin always resulted in lowering of their respective isoelectric points (pI). Employing cytochromes c derived from various sources, we examined a possible relationship between the degree of amino acid sequence degeneracy and the magnitude of change in the pI values by enzymatic methylation, and found that there was no correlation between these two parameters. By constructing space-filling models of oligopeptide fragments adjacent to the potential methylation sites, we have noted that not all the methylatable residues are able to form hydrogen bonds prior to the methylation. Two preparations of yeast apocytochrome c, one chemically prepared by removing heme from holocytochrome c and the other by translating yeast iso-1-cytochrome c mRNA in vitro, exhibited slightly higher Stokes radii than the homologous holocytochrome c, indicating relatively 'relaxed or open' conformation of the protein. However, when the in vitro synthesized methylated apocytochrome c was compared with the unmethylated counter-part, the Stokes radius of the latter was found to be larger.

• 한국식품영양학회지
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• 제3권2호
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• pp.149-160
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• 1990

The soybean $\beta$-amylase ($\alpha$-1, 4-glucan maltohydrolase, EC 3.2.1.2) is composed of seven isozymes(I', I, II, III, IV, V and VI), and isozyme II and IV are the main components among these. The Purification of $\beta$-amylase isozymes from soybean whey were performed by ammonium sulfate fractionation, CM-Sephadex C-50 column chromatography, DEAE-Sephadex chromatography and Gel filtration. The resulted purity of $\beta$-amylase was throughly confirmed by electrophoresis, and then determined its isoelectric point and molecular weight. The results obtained were as follows, 1. Five active fractions of soybean p-amylase were derived on CM-Sephadex C-50 column chromatography. 2. Seven active bands of p-amylase isozymes were detected by isoelectric focusing gel electrophoresis, and their isoelectric points(I' to VI) were 5.07, 5.15, 5.25, 5.40, 5.55, 5.70 and 5.93, respectively. 3. Isozyme II and IV were main components of soybean $\beta$-amylase. 4. The molecular weights of both isozyme II and IV were determined to be 56,000 daltons by the result of SDS polyacrylamide gel electrophoresis. 5. Km values of main isozyme II & IV for amylopectin were determined to be 2.25 mg/ml, which suggest the same function of each isozyme.