http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Purification and Characterization of Ice Nucleating Protein from Pseudomonas syringae
김정하,박순호,한문희,함경수,Kim, Jeong-Ha,Park, Soon-Ho,Han, Moon-H.,Hahm, Kyung-Soo 생화학분자생물학회 1989 한국생화학회지 Vol.22 No.1
Pseudomonas syringae로부터 빙핵활성을 갖는 단백질을 분리 정제하였다. 빙핵활성단백질은 균주로부터 분리한 세포외막에 비변성 계면활성제로 추출하고, Sephacryl S-400 크로마토그래피와 전기영동 용출법으로 정제하였다. 빙핵활성단백질은 분자량이 전기영동상에서 150,000 dalton 이었다. 빙핵활성의 측정은 모세관측정법을 사용하였고 정제된 단백질은 $-8^{\circ}C$에서 빙핵활성을 나타냈다. The protein responsible for ice-nucleation activity by Pseudomonas syringae AL (KCTC 1832) has been purified. The protein was purified from the outer membrane fraction of the cell by methods including extraction with non-denaturing detergents octyl-${\beta}$-D-thioglucopyranoside, gel filtration chromatography on Sephacryl S-400 and gel electroelution. The molecular weight of the ice-nucleating protein is estimated to be about 150,000 dalton by SDS-PAGE. Ice-nucleation activity was measured by the micro-pipette method. Ice-nucleation activity of the purified protein was about $-8{\sim}-9^{\circ}C$, whereas the freezing point of supercooled water is $-17^{\circ}C$.
Pseuomonas Syringae로 부터 빙핵활성단백질의 정제 및 특성에 관한 연구
김정하,박순호,한문희,함경수 ( Jeong Ha Kim,Soo Ho Park,Moon H . Han,Kyung Soo Hahm ) 생화학분자생물학회 1989 BMB Reports Vol.22 No.1
The protein responsible for ice-nucleation activity by Pseudomonas syringae AL (KCTC 1832) has been purified. The protein was purified from the outer membrane fraction of the cell by methods including extraction with non-denaturing detergents octyl-β-D-thio-glucopyranoside, gel filtration chromatography on Sephacryl S-400 and gel electroelution. The molecular weight of the ice-nucleating protein is estimated to be about 150,000 dalton by SDS-PAGE. Ice-nucleation activity was measured by the micro-pipette method. Ice-nucleation activity of the purified protein was about -8∼-9 ℃, whereas the freezing point of supercooled water is -17 ℃.