http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
- 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
- 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
RISS 인기검색어
- 검색키워드
- 저자 : 심우만 ( Jun Pyong Kim (검색결과 4 건)
- 무료
- 기관 내 무료
- 유료
-
김준평,안용근,심우만,Kim, Jun-Pyong,Ann, Yong-Geun,Shim, Woo-Man 생화학분자생물학회 1985 한국생화학회지 Vol.18 No.3
단시간에 고순도의 고구마 $\beta$-amylase 정제품을 얻을 수 있는 상온 아세톤 분획 결정법을 개발하고, 개발된 방법에 의해 정제 결정된 고구마 $\beta$-amylase의 물리화학적 특성을 일부 분석하여 다음과 같은 결과를 얻었다. Takeda와 Nakayama의 방법을을 조합 수정하여 상온 아세톤 분획으로 3시간 내에 고구마 $\beta$-amylase를 정제 결정하였다. 고구마 $\beta$-amylase는 26.3배 정제되어 4,395 unit/mg의 활성과 14.3%의 회수율을 나타냈고 결정은 직사각형의 판상(板狀)으로 행성되었다. UV difference spectrum 상에 불순물은 나타나지 않았고 polyacrylamide disc gel 전기영동에 의해 균일하게 나타났다. Maltase 및 $\alpha$-amylase 활성은 나타나지 않았고 전분에서는 maltose만 유리되었다. SDS polyacrylamide gel 전기영동에 의해 subunit의 분자량은 57,000으로 얻어졌고 아미노산 잔기는 약 478개로 추정되었다. Sweet potato $\beta$-amylase was purified and crystallized by the suggested acetone fractionation method at room temperature and some physicochemical properties of the enzyme were investigated. The enzyme was purified and crystallized by the suggested method in 3 hours, The purified enzyme showed 26,3 folds of purification, 4,395 unit/mg of specific activity and 14,3% of yield, respectively, compared to the crude extract. The crystallized enzyme was found to have a rectangular-sheet form in pure water. The purified enzyme was identified as homogenous by disc PAGE, UV difference spectrum, HPLC analysis and maltase activity assay, The molecular weight of the enzyme subunit was found to be 57,000 by SDS PAGE, The amino acid analysis indicated the enzyme is composed of 478 amino acid residues per 57,000 daltons of the enzyme subunit.
-
김준평,안용근,심우만 ( Jun Pyong Kim,Yong Geun Ann,Woo Man Shim ) 생화학분자생물학회 1985 BMB Reports Vol.18 No.3
Sweet potato β-amylase was purified and crystallized by the suggested acetone fractionation method at room temperature and some physicochemical properties of the enzyme were investigated. The enzyme was purified and crystallized by the suggested method in 3 hours. The purified enzyme showed 26.3 folds of purification, 4,395 unit/㎎ of specific activity and 14.3% of yield, respectively, compared to the crude extract. The crystallized enzyme was found to have a rectangular-sheet form in pure water. The purified enzyme was identified as homogenous by disc PAGE, UV difference spectrum, HPLC analysis and maltase activity assay. The molecular weight of the enzyme subunit was found to be 57,000 by SDS PAGE. The amino acid analysis indicated the enzyme is composed of 478 amino acid residues per 57,000 daltons of the enzyme subunit.
-
沈愚萬,崎山文夫,金正秀,吳文憲,戶田弘子,金俊平 中央大學校 食糧資源硏究所 1991 食糧資源硏究所 論文集 Vol.3 No.1
밀 β-amylase는 抽出液에 황산암모늄(70%)로 沈澱시켜 DADE-Cellulose, sephadex G-100 및 DEAE-sephadex A-50 chromatography로 精製한 바 두 分劃 A와 C를 얻을 수 있었다. 고구마 β-amylase는 acetone 濃度를 50%에서 沈澱시켜 다시 47%, 43%, 40%로 調節하면서 結晶化시켜 DEAE-sephadex A-25 chromatography로 單一 物質을 얻을 수 있었다. 밀 β-amylase와 고구마 β-amylase의 分子量은 β-amylase A 및 C 모두 54,000이며 고구마의 monomer의 分子量 57,000과 類似한 分子量임을 알 수 있었고, 다른 β-amylase인 콩 β-amylase의 分子量 57,000, 보리 56,000, 쌀 53,000, B. cereus 58,000과 거의 비슷한 分子量 5만 前後의 것임을 알 수 있었다. β-amylase의 아미노酸 組成의 특색으로는 모든 품종 공히 Asp., Glu.와 같은 酸性 아미노酸을 제일 많이 含有하고 있다는 것과 Thr., Ser., Ile. 및 Phe.의 中性 아미노酸이 콩, 밀, 고구마 β-amylase 중에 아미노酸 殘基數가 거의 비슷한 量이 들어 있음을 알 수 있었다. 고구마 β-amylase의 아미노酸 殘基數는 총 496殘基로, 이 結果 算出된 分子量은 55,707 임을 알 수 있었고 N-末端 아미노酸이 Ala.이고 C-末端 아미노酸이 Asp.임을 알 수 있었다. DOTMATRIX法에 의한 아미노酸 配列順序를 比較해 본 結果, 고구마 β-amylase와 콩 β-amylase의 아니노酸 配列順序가 가장 相同性이 높다. ALNED program에 의한 比較에 의하면 공시試料 6種類의 β-amylase를 통하여 적어도 6군데에 保存된 領域이 있음을 알 수 있었다. 品種間 β-amylase의 아미노酸 配列順序에서 아미노酸의 種類와 位置가 同一한 곳을 調査하여 보았더니, 고구마와 콩 β-amylase 중 63%에 해당한 312殘基가 같고 고구마와 보리의 β-amylase간의 相同性이 58%, 콩과 보리와의 相同性은 63.8%이다. 細菌 由來 β-amylase間에는 그 相同性이 80%인데 비해, 細菌由來 β-amylase와 다른 植物과의 相同性은 28%정도 밖에 안 된다. The major fraction of wheat β-amylase A and C were purified by using the method of ammonium sulfate fractionation(70%), ion-exchange chromatography with DEAE-cellulose, gel filtration with sephadex G-100 and chromatography with DEAE-sephadex A-50. The crude β-amylase extracted of sweet potato was purified by means of acetone fractionation(50-40%), crystallization and chromatography with DAEA-sephadex A-25. The molecular weight of the fraction A and C of wheat β-amylase was 54,000, and sweet potato β-amylase for monomer was 57,000, similary. On the other hand, molecular weight of soybean, barley, rice and Bac. cereus were 57,000, 56,000, 53,000 and 58,000, respectively. The amino acid profile of wheat, soybean and sweet potato β-amylase showed mostly acidic amino acid residues such as Asp. and Glu. The amino acid residues of soybean, sweet potato and wheat β-amylase showed same amount of neutral amino acids such as Thr. Ser. Ile. and Phe.. The amino acid residues of sweet potato β-amylase were 496 per mole of monomer and the molecular weight was calculated to be 55,707. The N-terminal and C-terminal amino acids of sweet potato were Ala. and Asp. respectively. In comparison of soybean and sweet potato β-amylase, the amino acid sequence of them determined by DOTMATRIX method showed similarity. The similarity of the β-amylase was proved by having 6 similar distribution of conserved regions with comparison of ALEND program. In evaluating the similarity between sweet potato and soybean β-amylase was the same sequence of 312 residues(63%), sweet potato and barley β-amylase 63% and bacterial and plant β-amylase 28% while that of bacterial β-amylases 80%.
-
김준평,심우만,김종익 한국농화학회 1980 Applied Biological Chemistry (Appl Biol Chem) Vol.23 No.1
White and black sesame produced in Korea were defatted with ethyl ether or n-hexane. Defatted sesame meal was extracted with water and salt solution, and protein extraction was precipitated at various pH 1 through 12, with trichloro acetic acid (TCA), tannic acid and ammonium sulfate, respectively. Protein was purified by Sephadex A-25, G-75, G-100 and G-200, and identified its protein fraction by polyacrylamide gel electrophoresis. Amino acids composition of protein in white sesame was analyzed by automatic amino acid analyzer. Protein contents of white sesame, black sesame and sesame meal are 20.5%, 19.2%, and 44.7%, respectively. n-Hexane was the most suitable solvent for extraction of oil from sesame. Crude protein precipitation was better in higher pH. The protein extraction was more effective with the solution containing sodium chloride under the pH 8. Globulin in total protein was high and prolamin was less than in other cereal proteins. Glutamic acid contents of white sesame and sesame globulin were 17.1%, and 20%, respectively. Both proteins contained relatively high levels of essential amino acids. 12-13 bands w ere found in water soluble protein and 2 bands in salt soluble protein were detected by the disc gel electrophoresis, and were identified in both of white and black sesame. The salt soluble protein of white sesame could be purified by Sephadee G-100 and G-200.
연관 검색어 추천
이 검색어로 많이 본 자료
활용도 높은 자료
