• 한국미생물·생명공학회지
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• 제30권4호
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• pp.320-324
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• 2002

우리나라 연안에 주로 발생되는 적조인 Cochlodinium polykrikoides를 빠르고 정밀한 생화학적인 방법으로 측정하기 위한 일종의 maker로서 C. polykrikoides의 세포막에 존재하는 특이 항원성을 가진 막 단백질을 분리하였다. 먼저, C. polykrikoides와 gymnodium sangineum의 세포를 삼투압으로 터뜨린 후 원심분리하여 세포막을 모았다. 그 후 양 적조생물의 세포막은 1 mM DTT가 함유된 50 mM Na-carbonate로 용해하고 SDS-PAGE행하여 용해된 막 단백질을 분리하였다. SDS-PAGE로 분리된 막 단백질은 C. polykrikoides의 세포 막 단백질로 제조한 항혈청을 사용하여 immune-blot한 결과 C. polykrikoides의 120 kDa의 단백질이 G. sangineum의 동일한 크기의 막 단백질과는 서로 다른 항원성을 나타내었다.

• 한국미생물·생명공학회지
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• 제18권5호
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• pp.517-524
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• 1990

CTAB/hexanol/isooctane 역미셀을 이용하여 단백질을 선택적으로 분리할 수 있는 분리조건을 밝히기 위해서 먼저 분자량과 등전점이 다른 여러 단백질의 용해와 회수에 미치는 pH, 이온의 종류 및 이온 강도, 계면활성제의 종류 등 system parameters에 대해 연구 검토하였다. pH에 따른 단백질의 용해는 등전점이 낮은 pepsin이 pH5-7 이상, 등전점이 높은 lisozyme이나 ribonuclease-a는 pH11-12 이상으로 단백질이 계면활성제의 (+)전하와 반대전하인 (-)를 띠는 등전점 이상의 pH역역에서 용해가 가능하였다.

• Clinical and Experimental Reproductive Medicine
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• 제27권4호
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• pp.381-385
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• 2000

Objective: To verify the effect of two forms (growth factor and growthfactor-reduced) of solubilized Matrigel on the development in mouse preimplantation embryos. Methods: Late 2-cell stage eggs were cultured through the blastocyst stage in the presence of GF- or GFR-Matrigel (0.5%, v/v). Morphological development, cell number and % apoptotic nuclei of blastocyst were measured by Roecst staining and TUNEL of nuclei. Results: Morphological development, number of cells per embryo was significantly increased in the presence of GF- or GFR-Matrigel. Culture of the embryos in the GF-Matrigel gave the best result. Conclusion: Low concentration of solubilized Matrigel improved development of mouse embryos regardless of growth factor content of the Matrigel. Growth factors and extracellular matrix protein included in the Matrigel synergistically potentiated the development of mouse embryos.

• Archives of Pharmacal Research
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• 제14권3호
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• pp.231-236
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• 1991

The high affinity binding sites for angiotensin II were solubilized from rat liver membranes by treatment with CHAPS. The binding protein was also partially purified by angiotensin III inhibitor-coupled Affi-gel affinity chromatography. Binding to the intact membrances as well as to the solubilized preparation was specific and saturable. According to the Scatchard plot, the membrane preparations exhibited a single class of high affinity binding sites with a Kd OF 0.71 nM. The solubilized preparation also showed the presence of a single class of bindings sites with less affinity (Kd of 14 nM). Meanwhile the competition studies using angiotensin II analogues represented two separate binding sites for angiotensin II and single binding site for antagonist. These latter findings were correlated to the results provided by Garrison's research group. More works are needed to clarify this discrepancy.

• 한국식품영양과학회지
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• 제14권1호
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• pp.82-87
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• 1985

닭의 가슴부위 및 다리부위의 골격근(骨格筋)에서 myofibril, actomyosin 및 myosin을 추출하고 ATPase activity(${\mu}mole$ pi/mg protein/min)로서 나타낸 몇가지 생물학적(生物學的) 활성(活性)을 비교하였다. 가슴부위에서 추출한 actomyosin, myofibril 그리고 myosin의 $Mg^{+2}$-ATPase 활성(活性)은 0.05M KCl에서 0.80, 0.42, 0.40으로서 다리부위에서 추출한 단백질(蛋白質)의 활성(活性)인 0.69, 0.33, 0.28 보다 높았다. 가슴부위와 다리부위의 myosin의 ATPase 활성(活性)은 EDTA 농도보다 $Mg^{+2}$농도가 높아지면서 ATPase 활성(活性)을 1/10정도 저해(沮害)시켰고, $Ca^{+2}$ 농도는 $10^{-3}M$에서 400%까지 활성(活性)을 증가시켰다. 가슴부위와 다리부위에서 추출한 actomyosin의 용해되는 시점(始點)은 각각 0.1M KCl 및 0.15 M KCl이었고 myosin인 경우는 각각 0.25 M KCi 및 0.30 M KCl이었다.

• Molecules and Cells
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• 제20권1호
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• pp.119-126
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• 2005

${\alpha}$-Expansins are bound to the cell wall of plants and can be solubilized with an extraction buffer containing 1 M NaCl. Localization of ${\alpha}$-expansins in the cell wall was confirmed by immunogold labeling and electron microscopy. The subcellular localization of vegetative ${\beta}$-expansins has not yet been studied. Using antibodies specific for OsEXPB3, a vegetative ${\beta}$-expansin of rice (Oryza sativa L.), we found that OsEXPB3 is tightly bound to the cell wall and, unlike ${\alpha}$-expansins, cannot be solubilized with extraction buffer containing 1 M NaCl. OsEXPB3 protein could only be extracted with buffer containing SDS. The subcellular localization of the OsEXPB3 protein was confirmed by immunogold labeling and electron microscopy. Gold particles were mainly distributed over the primary cell walls. Immunohistochemistry showed that OsEXPB3 is present in all regions of the coleoptile and root tissues tested.

• BMB Reports
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• 제46권9호
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• pp.471-476
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• 2013

The PIDDosome, which is an oligomeric signaling complex composed of PIDD, RAIDD and caspase-2, can induce proximity-based dimerization and activation of caspase-2. In the PIDDosome assembly, the adaptor protein RAIDD interacts with PIDD and caspase-2 via CARD:CARD and DD:DD, respectively. To analyze the PIDDosome assembly, we purified all of the DD superfamily members and performed biochemical analyses. The results revealed that caspase-2 CARD is an insoluble protein that can be solubilized by its binding partner, RAIDD CARD, but not by full-length RAIDD; this indicates that full-length RAIDD in closed states cannot interact with caspase-2 CARD. Moreover, we found that caspase-2 CARD can be solubilized and interact with full-length RAIDD in the presence of PIDD DD, indicating that PIDD DD initially binds to RAIDD, after which caspase-2 can be recruited to RAIDD via a CARD:CARD interaction. Our study will be useful in determining the order of assembly of the PIDDosome.

• Journal of Ginseng Research
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• 제20권3호
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• pp.274-283
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• 1996

In this study, the effects of red ginseng components [ginsenosides (total saponins and $Rg_1$) on the function of ryanodine receptor (RyR) -$Ca^{2+}$ release channel complex protein (named as RyR or $Ca^{2+}$ channel), a membrane protein in sarcoplasmic reticulum (SR) of rabbit skeletal muscle were examined at the SR vesicle's level and the molecular levels with Chaps-solubilized and purified $Ca^{2+}$ channel protein and with reconstituted proteoliposomes by dialysis. The results were as follows. 1. The binding of ryanodine known as inhibitor of muscle contraction to the RyR was decreased at the whole range of concentration ($10^2$~$10^7$%) by these two ginseng components. In heavy SR vesicles, Chaps-solubilized and purified $Ca^{2+}$ channel protein, and reconstituted vesicles, its maximal inhibition by total saponins was shown at the concentration of $10^3$, $10^3$%, and $10^5$% respectively, and by gin- senoside $Rg_1}$) each was $10^3$%, $10^3$%, and $10^4$%. 2. The release of $Ca^{2+}$ ion through $Ca^{2+}$ channel in heavy SR vesicles and reconstituted proteoliposomes was increased as a whole by these two ginseng components, and particularly maximal release by both of them was shown at the range of $10^4$~$10^6$%. These results were seemed to be caused by conformational change of $Ca^{2+}$ release channel protein (RyR) by red ginseng components [ginsenosides (total saponins and $Rg_1}$).

• 약학회지
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• 제42권1호
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• pp.46-52
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• 1998

Retroviral integrase is required for integration of viral DNA into the host cell chromosome. Human immunodeficiency virus type-1 integrase was partially purified as a part of a fusion protein linked to a maltose-binding protein and characterized in terms of an endonucleolytic activity. The concentration of the fusion protein purified through an amylose column was about 12mg/ml. Indicating that the solubility of the fusion protein is highly increased by the presence of a maltose-binding protein, considering that the integrase protein alone is poorly solubilized. The endonucleolytic activity of the fusion protein was detected at 0.1 to 1.OmM $Mn^{++}$ ion, but not at any concentrations tested of $Mn^{++}$ ion.

• 한국수산과학회지
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• 제33권5호
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• pp.413-417
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• 2000

생분해성이면서 가식성인 어분 단백질필름 제조를 목적으로 필름의 가공조건이 단백질필름의 성질에 미치는 영향을 밝히기 위하여 명태어분으로부터 단백질을 추출하고, 가공조건을 달리하여 제조한 필름의 수증기 투과도와 용해도의 변화를 측정한 결과는 다음과 같다. APMPI 필름의 수증기 투과도는 가소제 glycerol의 첨가량이 증가함에 따라 증가였으나, pH 7 이상에서는 pH의 증가에 따라 감소하였다. 필름단백질의 용해도는 pH 및 가소제의 농도가 증가함에 따라 감소하였다. 필름의 총용해량은 가소제의 농도가 증가함에 따라 증가하였으나 pH가 증가할수록 감소하였다 가소제의 종류를 달리하여 필름을 제조할 때 수증기 투과도는 glycerol, polyethylene glycol 및 sorbitol 첨가 필름의 차례로 높게 나타났다. 또한 총용해량은 반대의 순서를 나타내었다.