• 폴리머
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• 제26권2호
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• pp.279-286
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• 2002

기능성고분자표면으로 개질하기 위해서 polyethylene(PE)표면에 아크릴산을 알곤 플라즈마를 이용하여 고정화와 그라프팅을 행하고 고정화와 그라프딩에 의한 개질효과를 ATR적외선스펙트럼의 분석, 접촉각과 접착강도 측정에 의하여 평가하였다. 아크릴산의 특성흡수띠와 접촉각의 현저한 감소사실로부터 친수성개질을 평가하였다. 그라프팅된 PE의 접촉각은 플라즈마처리시간에 따라서 무처리 PE에 비하여 47~$53^{\circ}$ 감소하였고 고정화된 PE는 이보다 작은 23~$26^{\circ}$ 감소하여 그라프팅이 고정화보다 더 효과적인 친수화 수단이 됨을 관찰할 수 있었다. 표면친수화의 정도는 플라즈마 처리시간과 방전출력에 강하게 의존하였다. 그라프팅의 경우 처리시간이 증가할수록 더욱 친수화되지만 고정화의 경우는 처리시간의 증가와 방전출력의 증가는 오히려 친수성을 감소시켰다. 개질된 PE표면의 peel test에 의한 접착강도측정 전파 역시 접촉각과 같은 경향을 나타내었다. 이러한 현상은 고정화과정 중에 아크릴산이 ablation되어 표면의 카복시친수성기가 감소하는 현상 때문으로 해석되었다.

• 폴리머
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• 제26권1호
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• pp.28-36
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• 2002

본 연구에서는 바이오칩 등에 응용 가능한 전도성 고분자 필름을 제조하기 위해 3-triophene acetic acid을 선택하여, 쉽게 전기적으로 산화되어 전기적 활성을 나타내는 고분자들을 형성하였다. 3-Thiophene acetic acid에 있는 카르복실기의 보호기들은 solid state에서 쉽게 제거되어질 수 있고, 그 결과 반응성 카르복실기가 전기적 활성을 나타내는 고분자 표면 위에 재생되어질 수 있었다. 즉, 카르복실기의 보호를 통한 전기중합과 뒤이은 보호기의 제거로 반응성인 카르복실기를 갖는 새로운 고분자 담체를 제조할 수 있었고, 기존의 방법으로 합성한 macromonomer를 필름 표면에 도입하여 전기적 활성을 나타내며 동시에 고분자 전해질이 도입된 전도성 고분자 필름을 얻었다. 합성한 전도성 단량체들과 macromonomer의 도입여부는 FT-IR과 $^1H-NMR$ 및 ESCA측정으로 확인하였고, 전극표면에 형성된 필름들의 형태는 SEM을 통해서 관찰하였다. 전기적 활성은 cyclic voltammogram(CV)을 통하여 확인하였으며, 얻어진 고분자 필름들은 0.7~0.9 V의 영역에서 전형적인 poly(3-alkylthiophene)의 전기 화학적 거동을 나타내었다.

• Korea Journal of Cosmetic Science
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• 제2권1호
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• pp.11-19
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• 2020

The aim of this study is to investigate the effect of various pentapeptides on hair repair depending on the characteristics of comprising amino acids using crosslinking agents in hair. Total ten peptides were synthesized with two kinds of amino acids respectively, of which were previously categorized according to R group of the amino acids contributing to the characteristic of each peptide: STTSS (Ser-Thr-Thr-Ser-Ser), LIILL (Leu-Ile-Ile-Leu-Leu), CMMCC (Cys-Met-Met-Cys-Cys), DEEDD (Asp-Glu-Glu-Asp-Asp), RKKRR (Arg-Lys-Lys-Arg-Arg), TAMRA-STTSS, TAMRA-LIILL, TAMRA-CMMCC, TAMRA-DEEDD, and TAMRA-RKKRR. Pentapeptide alone, or pentapeptides with crosslinking agents such as polymeric carbodiimide (PCI) and 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) were treated to chemically damaged hair. Hair diameter and break strength (N = 40/case) were measured to calculate tensile strength of hair for computing hair repair ratio, and fluorescence yields (N = 20/case) were collected for hair treated with TAMRA-peptides. The tensile strength of hair treated with pentapeptides alone, or pentapeptides with cross-linking agents is consistent with the fluorescence yield from the microscope images of the cross-sectioned hair in vision and in numerical values. Pentapeptides consisting of hydrophobic amino acids (LIILL), amino acids with sulfur (CMMCC), and basic amino acids (RKKRR) increased the tensile strength in perm-damaged hair. Pentapeptides with no extra carboxyl/amine groups in R group of amino acids resulted in no significant differences in hair strength and fluorescence yield among hairs treated with alone and with crosslinkers. Pentapeptides with extra carboxyl groups or amine groups enabled further strengthening of hair due to increased bonds within the hair after carbodiimide coupling reaction. The hair repairs of pentapeptides with various amino acid sequences were studied using crosslinking. Depending on the physical characteristics of comprising amino acids, the restoration of damaged hair was observed with tensile strength of hair and fluorescence signals upon cross-sectioned hair in parallel to possibly understand the binding tendency of each pentapeptide within the hair.

• The Korean Journal of Physiology
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• 제10권1호
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• pp.15-24
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• 1976

The action of aconite on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of aconite on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by aconite, and the concentration of aconite for maximal activity is about 80 mg%. The pH optimum for the aconite sensitive component is 8.0. 2. The activating effect of aconite on the ATPase, with a given concentration of sodium in the medium, is increased by raising the potassium concentration but activity ratio is decreased. 3. The activating effect of aconite on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 4. The action of aconite on the ATPase activity is inhibited by calcium ions and the effect of inhibition is increased by small amounts of calcium but decreased by larger amounts. 5. The activating effect of aconite on the ATPase was not related to the sulfhydryl group of cysteine, the amino group of lysine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The action of aconite on the ATPase activity is due to carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• 제8권1호
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• pp.67-76
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• 1974

The effect of saponin on the sodium plus potassium activated ATPase activity was studied in the rabbit red cell ghosts and the experiments were also designed to determine the mechanism of action of saponin on the APTase activity. The following results were observed. 1. The ATPase activity of rabbit red cell ghosts is inhibited by low concentration of saponin but increased by high concentration. The activating effect of saponin on the $Na^{+}-K^{+}-ATPase$ activity is inhibited by ouabain but the stimulation of the $Mg^{++}-ATPase$ by high concentration of saponin is not inhibited by ouabain. 2. The activity ratio of $Na^{+}-K^{+}-ATPase$ by high concentration of saponin is decreased by raising the potassium concentration, and is increased by raising the sodium concentration. 3. The ATPase activity is increased by small amounts of calcium but inhibited by larger amounts. The activity ratio of the enzyme by saponin is decreased by raising the calcium concertration 4. The action on the ATPase activity was not related to the amino group of lysine, the hydroxyl group of threonine, the imidazole group of histidine, or the carboxyl group of aspartic acid. 5. The action of saponin on the ATPase activity is due to sulfhydryl group of the enzyme of $Na^{+}-K^{+}-ATPase$.

• The Korean Journal of Physiology
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• 제12권1_2호
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• pp.25-34
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• 1978

The action of theobromine on the sodium plus potassium activated ATPase activity In the rabbit red cell membrane has teen investigated and the experiments were also designed to determine the mechanism of action of theobromine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red fell membrane is stimulated by theobromine, and the concentration of theobromine for maximal activity is about 3mM. 2. The activating effect of theobromine on the ATPase, with a given concentration of potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased. 3. The activating effect of theobromine on the ATPase, with a given concentration of sodium in the medium. is increased by the raising the potassium concentration but activity ratio is decreased. 4. The NaK ATPase activity is increased by small amounts of calcium but decreased by larger amounts. The activity of the enzyme by theobromine is increased by small amounts of calcium but decreased by larger amounts. 5. The activating effect of theobromine on the ATPase was not related to the hydroxyl group of threonine and imidazole group of histicline. 6. The activating effect of theobromine on the ATPase is due to sulfhydryl group, amino group and carboxyl group of the enzyme of NaK ATPase.

• The Korean Journal of Physiology
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• 제11권1호
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• pp.11-20
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• 1977

The action of pilocarpine on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of pilocarpine on the ATPase activity. The following results were observed. 1. The activity of the NaK ATPase from red cell membrane is stimulated by pilocarpine, and the concentration of pilocarpine for maximal activity is about 3 mM. The pH optimum for the pilocarpine sensitive component is 8.0. 2. The activating effect of pilocarpine on the ATPase, with a given concentration of sodium .in the medium, is increased by raising the potassium concentration but activity ratio is decreased 3. The activating effect of pilocarpine on the ATPase, with a given concentration of Potassium in the medium, is increased by raising the sodium concentration but activity ratio is decreased 4. The NaK ATPase activity is increased by small amounts of calcium but decreased by 'larger amounts. The activity ratio of the enzyme by pilocarpine is decreased by small amounts .of calcium but decreased by larger amounts. 5. The activating effect of pilocarpine on the ATPase was not related to the sulfhydryl group of cysteine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The activating effect of pilocarpine on the ATPase is due to amino group and carboxyl group of the enzyme of NaK ATPase

• The Korean Journal of Physiology
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• 제11권1호
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• pp.1-9
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• 1977

Action of anthraquinone on the sodium plus potassium activated ATPase activity in the rabbit red cell membrane has been investigated and the experiments were also designed to determine the mechanism of action of anthraquinone on the ATPase activity. The following results were obtained 1. The activity of the NaK ATPase from red cell membrane is inhibited by anthraquinone and the concentration of anthraquinone for maximal inhibition is about 5mM. 2. The ratio of inhibition of NaK ATPase by anthraquinone, with a giving concentration of sodium in the medium, is increased by raising the potassium concentration. 3. The ratio of inhibition of NaK ATPase by anthraquinone, with a given concentration of potassium in the medium, is increased by raising the sodium concentration. 4. The action of anthraquinone on the NaK ATPase activity is inhibited by calcium ions and the ratio of inhibition is increased by small amounts of calcium but almost constant by larger amounts. 5. The inhibitory action of anthraquinone on the NaK ATPase activity was not related to the amino group of lysine, the hydroxyl group of threonine or the imidazole group of histidine. 6. The inhibitory action of anthraquinone on the ATPase activity is due to sulfhydryl group or the carboxyl group of the enzyme of NaK ATPase.

• 한국생물공학회:학술대회논문집
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• 한국생물공학회 2003년도 생물공학의 동향(XII)
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• pp.635-638
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• 2003

For the acute assessment on biological toxicity of wastewater, surface plasmon resonance(SPR) based cell viability detection was performed using gold surface-confined cell as a result of adhesion-modifying chemicals. Escherichia coli O157:H7 (E. coli O157:H7) was investigated after exposure to EDTA. Cells were immobilized on gold coated slide glass for SPR analysis by the method of cross-linking carboxyl group on the bacterial surface with amine group of poly-L-lysine that had been coupled to the gold surface modified by a self-assembled monolayer of 11-mercaptounde canoic acid (11-(MUA)). Reflective intensity of each flow step was changed with respect to confect of ethylenediaminetetraacetic acid (EDTA) disodium salt and phosphate-buffered saline (PBS) solution. The proposed detection technique can be used for biological toxicity test.

• 펄프종이기술
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• 제30권2호
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• pp.55-61
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• 1998

This treatment was applied to bleached softwood kraft pulp handsheets in an effort to improve physical strength of paper. Paper strength was improved by esterification of cellulose and polycarboxylic acid. Because hydrogen bond of carboxyl group is stronger than that of hydroxyl group, polycarboxylic acid forms stronger hydrogen bond than cellulose does. 1,2,3,4,-cyclopentanetetracarboxylic acid (CPTA) and sodium dihydrogen phosphate ($NaH_2O_4$) were used as polycarboxylic acid and catalyst, respectively This reaction was confirmed by the weight gain of the handsheets, by FTIR spectrum and by changes in mechanical properties of sheets. Wet tensile strength was improved when handsheets were treated with polycarboxylic acid. However, tear strength and burst strength decreased.