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.
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 ...
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.
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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