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2D NMR Probe Development for Investigation of Biosupramolecular Systems
김안드레,강신원,박장수 한국자기공명학회 2004 Journal of the Korean Magnetic Resonance Society Vol.8 No.1
Biosupramolecular systems such as biological membranes usually fluid under physiological conditions1. Therefore, solid-state NMR has been used to investigate biosupramolecular systems. But solid-state NMR spectra contain a large number of overlapping resonances and are rather difficult to analyze. These problem has to be overcome by selective isotope labeling. We constructed a deuterium NMR probe for AM400 NMR spectrometer, which is mainly used for liquid samples. To overcome the fluidity problem, a saddle type coil was designed. The efficiency was systematically investigated for two kinds of coil geometry, solenoid and saddle types. Our results suggest that solenoids are superior to saddle type coils in the sensitivity. However, the letter fits better to fluid samples such as biosupramolecular systems 영어논문
Nitrogen Isotope Labeled Tetraheme Cytochrome c3 on a Defined Medium
김안드레,Jang-Su Park* 대한화학회 2005 Bulletin of the Korean Chemical Society Vol.26 No.2
To obtain cytochrome c3 labeled with a stable isotope, the conditions of cultivation and the composition of medium for DvMF were examined. The growth of DvMF was steady and reproducible under purging with N2 and under pH control. DvMF was able to go on a defined medium without natural products. The composition of medium containing a small amount of NH4Cl as sole nitrogen source was established. Then, uniformly 15N-labeled cytochrome c3 was obtained during the culture of DvMF in a defined medium with 15NH4Cl; it was confirmed by 1H-15N HMQC.
김안드레,박장수 한국분자세포생물학회 2002 Molecules and cells Vol.13 No.3
The eukaryotic replication protein A (RPA) is a heterotrimeric protein complex. It consists of 70, 32, and 14 kDa subunits that are involved in DNA replication, repair, and genetic recombination. RPA is a 4-cysteine type zinc-finger protein. RPA’s zinc-finger domain is not essential for DNA binding activity, but it is involved in the regulation of RPA’s DNA binding activity through reduction-oxidation (redox). In this study, we show that yeast RPA’s ssDNA binding activity is regulated by redox potential through its subcomplexes of 32 and 14 kDa subunits. In contrast, the subunits’ complex, RPA70, formed a stable complex with ssDNA, even under non-reducing conditions. The addition of DTT and H2O2 had no effect on its DNA binding activity. In RPA70, since the addition of the subcomplexes of the 32 and 14 kDa subunits, it restored the modulating ssDNA binding activity to native RPA’s DNA binding activity. These results suggest that the subcomplexes of the 32 and 14 kDa subunits may be involved in the modulating RPA’s DNA binding activity through redox change. These studies, therefore, show the novel structure and function relationship of a multiprotein complex in that the role of a specific domain (or one subunit) is regulated by the other subunits.
NMR Studies on Ferricytochrome c3 and its Interaction with Ferredoxin I
김안드레,박장수 한국자기공명학회 1999 Journal of the Korean Magnetic Resonance Society Vol.3 No.1
The 1H NMR signals of the heme methyl, propionate and related chemical groups of cytochrome c3 from Desulfovibrio vulgaris Miyazaki F (D.v. MF) were assigned by means of 1D NOE, 2D DQFCOSY and 2D TOCSY spectra. They were consistent with the assignments of the hemes with the highest and second-lowest redox potentials reported by Gayda et al. [Reference: 15]. The heme assignments were also supported by NOE between the methyl groups of these hemes and the side chain of Val-18, All the results contradicted the heme assignments for D.v. MF cytochrome c3 made on the basis of NMR [Reference: 11]. Based on these assignments, the interaction of cytochrome c3 with ferredoxin I was investigated by NMR. The major interaction site of cytochrome c3 was identified as the heme with the highest redox potential, which is surrounded by the highest density of positive charges. The stoichiometry and association constant were two cytochrome c3 molecules per monomer of ferredoxin I and 108 M-2 (at 53 mM ionic strength and 25 oC), respectively. 영어논문
한국산 길조류에서 추출한 Fucoidan의 황산기에 따른 항암작용
박장수,김안드레,김은희,서홍숙,최원철,Park, Jang-Su,Kim, An Deu Re,Kim, Eun-Hui,Seo, Hong-Suk,Choe, Won-Cheol 대한화학회 2002 대한화학회지 Vol.46 No.2
Fucoidan은 갈조류에 다량 함유되어있는 다당류로서 항암작용, 항혈응고작용, 항혈전작용, 항염증작용, 항virus작용과 같은 생리활성작용력을 가지고 있어 최근 많은 연구가 수행되어지고 있다. 본 논문은 갈조류에서 fucoidan을 추출 하여 그 항암활성을 SV40 DNA replication assay, RPA-ssDNA binding assay, 그리고 MCF7 cell growth inhibition assay를 이용하여 알아보았으며 이 항암활성은 fucoidan의 황산기가 중요한 역할을 하고 있음을 알아내었다. 화학적으로 황산기의 함유량을 증가시킨 fucoidan이 황산기의 함유량을 제거시킨 fucoidan보다 항암활성이 뛰어났고, 이는 RPA의 ssDNA 결함력을 떨어 EM리기 때문이라 예측되어 진다. 본 연구는 한국산 갈조류에서 추출한 황산기를 함유한 fucoidan의 항암활성능력을 보여주었다. Fucoidan is a kind of polysaccharides in brown seaweeds. For the past years have been extensively studied due to their numerous biological activities : anticancer, anticoagulant, antithrombotic, anti-inflammatory and antiviral. In this study, we h ave extracted fucoidan from the Korean brown seaweeds and examined it's anticancer activities for employed SV40 DNA replication assay, RPA-ssDNA binding assay of replication protein A(RPA: known as human single-stranded DNA-binding protein essential for DNA rep-lication) and MCF7 cell growth inhibition assay. In addition to, we found that chemically sulfated fucoidan'santicancer activity is more higher than natural and desulfated fucoidan. It seem that fucoidan's sulfate group affect on DNA replication, cause of decrease RPA's DNA binding activity. These results suggests that sulfated fucoidan from Korean brown seaweeds have anticancer activity.