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RISS 인기검색어
- 검색키워드
- 저자 : 함경수 ( Myeong Kyu Lee (검색결과 6 건)
- 무료
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이명규,함경수 ( Myeong Kyu Lee,Kyung Soo Hahm ) 생화학분자생물학회 1986 BMB Reports Vol.19 No.4
Radial immunodiffusion (RID) was used for determination of apolipoprotein B in LDL, VLDL, and plasma. The method closely approximated the values of LDL apo B obtained by the standard Lowry procedure (r=0.968). Using 1% agarose in the method made it feasible to estimate plasma and VLDL apo B levels. The present study also shows that plasma total cholesterol level correlates well (r=0.981) with the plasma apo B level measured by the RID method.
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Quantitation of Human Plasma Apoprotein B by Radial Immunodiffusion
이명규,함경수,Lee, Myeong-Kyu,Hahm, Kyung-Soo 생화학분자생물학회 1986 한국생화학회지 Vol.19 No.4
Radial immunodiffusion (RID)방법을 이용하여 LDL, VLDL 및 혈장에 존재하는 apoliporprotein B의 농도를 측정하였다. LDL apo B 의 농도를 본 방법과 단백질 정량 방법으로 흔히 사용되는 Lowry의 방법으로 측정, 비교하여 보았을 때 차이가 없었다 (r=0.968). Agarose 의 농도를 1%로 함으로써 VLDL 과 혈장의 apo B의 농도 또한 측정이 가능하였으며, 본 방법으로 측정한 혈장의 apo B 농도와 혈장 콜레스테롤 농도를 비교해 보았을 때 의의있는 상관관계(r=0.981)가 있었다. Radial immunodiffusion (RID) was used for determination of apolipoprotein B in LDL, VLDL, and plasma. The method closely approximated the values of LDL apo B obtained by the standard Lowry procedure (r=0.968). Using 1% agarose in the method made it feasible to estimate plasma and VLDL apo B levels. The present study also shows that plasma total cholesterol level correlates well (r=0.981) with the plasma apo B level measured by the RID method.
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인체 간세포 표면에 존재하는 쥐의 간암의 특이 항원에 대한 면역학적 규명
이명규,한문희,함경수 ( Myeong Kyu Lee,Moon H . Han,Kyung Soo Hahm ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.4
Hepatocellular carcinoma was induced in Sprague-Dawley rats using 2-MeDAB and DENA, and hepatoma associated antigens were identified and isolated from the plasma membrane surface of rat liver. Rabbit antisera against hepatoma associated antigens were obtained and reactivity of the antibody with proteins extracted from human livers (normal and hepatoma) was analyzed by double immunodiffusion, immunoelectrophoresis and crossed-immunoelectrophoresis. The results showed a strong evidence for the presence of proteins (MW 65,000 & 55,000) on the human liver cell cross-reacting with the antibody against rat hepatoma associated antigens. These human proteins were found to be unreactive with the antiserum against plasma membrane surface proteins of normal rar liver.
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Immunological Identification of Rat Hepatoma Associated Antigens on Human Liver
이명규,한문희,함경수,Lee, Myeong-Kyu,Han, Moon-H.,Hahm, Kyung-Soo 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.4
화학 발암제인 2-MeDAB 및 DENA를 투여함으로서 Sprague-Dawley 쥐에 간암을 유발시켰으며, 간암세포 원형질막 표면으로부터 간암 특이 항원을 분리하였다. 쥐의 간암 특이 항원에 대한 항체를 토끼로부터 분리하였으며, 이 항체와 사람의 정상간 및 간암세포 표면에서 분리한 단백질과의 반응을 double immunodiffusion, 면역 전기영동법 및 교차변역 전기영동법 등을 이용하여 분석하였다. 그 결과 사람의 간 세포 원형질막 표면에 쥐의 간암 특이 항원에 특이한 항체와 반응하는 단백질(분자량 65,000 및 55,000)이 존재함을 확인하였다. 한편 이 단백질은 쥐의 정상 간세포 표면 단백질에 대한 항체와는 반응하지 않았다. Hepatocellular carcinoma was induced in Sprague-Dawley rats using 2-MeDAB and DENA, and hepatoma associated antigens were identified and isolated from the plasma membrane surface of rat liver. Rabbit antisera against hepatoma associated antigens were obtained and reactivity of the antibody with proteins extracted from human livers (normal and hepatoma) was analyzed by double immunodiffusion, immunoelectrophoresis and crossed-immunoelectrophoresis. The results showed a strong evidence for the presence of proteins (MW 65,000 & 55,000) on the human liver cell cross-reacting with the antibody against rat hepatoma associated antigens. These human proteins were found to be unreactive with the antiserum against plasma membrane surface proteins of normal rar liver.
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재조합 인체 인터루킨 - 2 1 . 분리정제 및 생화학적 특성
윤혜영,최혜림,이명규,김승호,나도선,이선복,한문희,함경수 ( Hye - Young Yun,Hye - Lim Choi,Myeong Kyu Lee,Seung Ho Kim,Doe Sun Na,Sun Bok Lee,Moon H . Han,Kyung - Soo Hahm ) 생화학분자생물학회 1988 BMB Reports Vol.21 No.2
Recombinant human interleukin-2 (rH IL-2, Ser^(125)-rH IL-2) was purified to apparent homogeneity from E. coli in high yield and characterized its biochemical properties for the establishment of preclinical screening system and therapeutic applications. The purification was carried out by methods involving isolation of inclusion body, urea extraction, solubilization and gel filtration chromatography. The renaturation of the product was achieved by extensive dialysis against the storage buffer. The purity was confirmed by SDS-PAGE and HPLC. Amino terminal amino acid analysis and partial amino acid sequence analysis showed that the primary structure of the recombinant protein (rH IL-2) was found to be identical with natural IL-2. The purity and the conformation of the rH IL-2 were also confirmed by obtaining crystals of the recombinant protein.
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Recombinant Human Interleukin-2: I. Purification and Biochemical Characterization
윤혜영,최혜림,이명규,김승호,나도선,이선복,한문희,함경수,Yun, Hye-Young,Choi, Hye-Lim,Lee, Myeong-Kyu,Kim, Seung-Ho,Na, Doe-Sun,Lee, Sun-Bok,Han, Moon-H.,Hahm, Kyung-Soo 생화학분자생물학회 1988 한국생화학회지 Vol.21 No.2
유전자 재조합 방법에 의해서 대장균으로 부터 재조합 인체 인터루킨-2 (rH IL-2, $Ser^{125}$-rH IL-2)를 과발현 시켰으며, 이 재조합 인체 인터루킨-2를 순수분리하여 그 생화학적 특성을 조사하였다. 분리 및 정제는 세포봉입체의 분리, 우레아 추출, 용해 및 젤여과 크로마토그라피 등을 사용하였으며, 정제된 인터루킨-2의 원형재현은 투석법을 사용하였다. 정제된 재조합 인터루킨-2의 순도는 전기영동 및 HPLC로 확인하였으며, 또한 결정을 얻음으로써 재확인하였다. 아미노말단 아미노산분석 및 아미노산배열순서를 일부 결정함으로서 정제된 재조합 인체 인터루킨-2가 천연 인터루킨-2와 동일한 일차구조를 갖고 있음을 확인하였다. Recombinant human interleukin-2 (rH IL-2, $Ser^{125}$-rH IL-2) was purified to apparent homogeneity from E. coli in high yield and characterized its biochemical properties for the establishment of preclinical screening system and therapeutic applications. The purification was carried out by methods involving isolation of inclusion body, urea extraction, solubilization and gel filtration chromatography. The renaturation of the product was achieved by extensive dialysis against the storage buffer. The purity was confirmed by SDS-PAGE and HPLC. Amino terminal amino acid analysis and partial amino acid sequence analysis showed that the primary structure of the recombinant protein (rH IL-2) was found to be identical with natural IL-2. The purity and the conformation of the rH IL-2 were al so confirmed by obtaining crystals of the recombinant protein.
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