• 대한약침학회지
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• 제25권1호
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• pp.52-62
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• 2022

Objectives: Snake venom is a complex mixture of various pharmacologically active substances, such as small proteins, peptides, and organic and mineral components. This paper aims to identify and analyse the proteins in common venomous snakes, such as Gloydius blomhoffii (G. blomhoffii) and Agkistrodon acutus (A. acutus), in Korea. Methods: We used mass spectrometry, electrophoresis, N-terminal sequencing and in-gel digestion to analyse the proteins in these two snake venoms. Results: We identified eight proteins in G. blomhoffii venom and four proteins in A. acutus venom. The proteins detected in G. blomhoffii and A. acutus venoms were phospholipase A₂, snake venom metalloproteinase and cysteine-rich secretory protein. Snake C-type lectin (snaclec) was unique to A. acutus venom. Conclusion: These data will contribute to the current knowledge of proteins present in the venoms of viper snakes and provide useful information for investigating their therapeutic potential.

• BMB Reports
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• 제39권5호
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• pp.556-559
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• 2006

The Bcl-2 family of proteins regulates mitochondrial functions during cell death by modulating the efflux of death-promoting proteins such as cytochrome c and endonuclease G. Upon the binding of death ligands to their receptors, caspase-8 cleaves Bid, a BH3-only protein, into tBid that causes the mitochondrial damages resulting in the release of cytochrome c and endonuclease G. Also, another BH3-only protein, hNoxa, has been shown to induce the efflux of cytochrome c from the mitochondria. Whether the efflux proteins from the mitochondria in response to tBid or hNoxa are the same or different, however, has not been addressed. We have demonstrated that endonuclease G activities are not detectable among the proteins released from isolated mitochondria by hNoxa but are detectable in that by tBid. These results suggest that the efflux of proteins from the mitochondria are differentially modulated by tBid and hNoxa.

• Journal of Nutrition and Health
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• 제9권2호
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• pp.87-97
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• 1976

This study is based on data from the food consumption survey on 727 members of 125 farm households from 7 different provinces. The survey was conducted in May, 1975 in cooperation with the O.R.D. The results obtained in this study are summarized as follows. 1. The average consumption of the basic food groups per capita per day was 563 g for cereals and grains(398g of rice and 129g of barley), 87.6g for meats and legumes, 317.8g for fruits and vegetables, 25.7g for milks and small fishes, 9.1g for fats and oils, and 45.1g for other group. 2. The average daily consumption of calories and nutrients was 2256 cal and 11.7g for animal proteins, 70.5g for total proteins, 21.6g for fats, 537.4mg for calcium, 18.1mg for iron, 5375lU for vitamin A, 1.27mg for thiamine, 1.05mg for riboflavin, 15.5mg for niacin, 77.7mg for ascorbic acid. When these figures are compared with the recommended allowances for Korean, the calories and nutrients intakes were satisfactory, except for the intakes of animal protein which was below two third of the recommended allowance. 3. The diets of the projected villages differed from those of the non-projected villages in the following respect: (a) The amounts of animal proteins and fats were larger in the projected villages than in the non-projected villages. (b) The percentage contribution of fats to the total amount of calories from three nutrients, carbohydrates, proteins and fats was higher in the projected villages than in tile non-projected villages. (c) The percentage contribution from carbohydrates to the total amount of calories was higher in the non-projected villages than in the projected villages. 4. Certain physical and clinical symptoms were observed among the people in the rural areas, which can be related to the shortages of animal proteins and fats in their diets. It is recommended to pay special attention to the nutrition of school children in the Korean rural areas.

• 대한의생명과학회지
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• 제9권3호
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• pp.159-165
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• 2003

Ankyrins are a ubiquitously expressed family of intracellular adaptor proteins involved in targeting diverse proteins to specialized membrane domains in both the plasma membrane and the endoplasmic reticulum. Recently, the studies with C-terminus of ankyrins have identified that ankyrin-B is capable of interacting with Hsp40 and sAnkl is capable of interacting with obscurin and titin, but the function of C-terminal domain of ankyrin-G remains unknown. To identify proteins interacting C-terminus of ankyrin-G, we used the C-terminus of ankyrin-G as a bait for a yeast two-hybrid screen of brain cDNA library. Approximately 1.33$\times$l0$^6$ transformants were screened, of which 13 positive clones were obtained as determined by activation of HIS3, ADE2 and MELl reporter genes. Sequence analyses of these 13 plasmids revealed that cDNA inserts of 13 colonies showed highly homologous to 11 genes, including 5 known (i.e., Na$^+$/K$^+$ ATPase $\beta$1, SERBPl, UTF2, cytochrome C oxidase and collagen IV $\alpha$2) and 6 unknown genes. The evaluation of the proteins that emerge from these experiments provides a rational approach to investigate the those proteins significant in interaction with ankyrin-G.

• 생명과학회지
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• 제20권8호
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• pp.1166-1172
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• 2010

Kinesin-I은 4분자의 단백질로 구성되어 있으며, N-말단의 motor 영역과 C-말단영역을 가지는 장쇄(KHC, 또한 KIF5s로도 통용) 2분자와 KIF5s (KIF5A, KIF5B와 KIF5C)의 줄기영역과 결합하는 단쇄(KLC) 2분자로 구성되어 있다. KIF5A의 결합 단백질을 동정하기 위하여 효모 two-hybrid system을 사용하여 특이적으로 결합하는 heterotrimeric G 단백질의 ${\beta}$ 단위체 단백질($G{\beta}$)을 분리하였다. $G{\beta}$은 KIF5A의 808에서 935아미노산 부위와 결합하며, 다른 KIF5들과도 결합함을 효모 two-hybrid assay로 확인하였다. 또한 $G{\beta}$의 WD40 반복 서열은 KIF5A와의 결합에 필수영역임을 확인하였으며, 이러한 단백질간의 결합은 Glutathione S-transferase (GST) pull-down assay를 통하여 확인하였다. 생쥐의 뇌 파쇄액에 KIF5들의 항체로 면역침강을 행하여 heterotrimeric G 단백질을 확인한 결과, KIF5들은 heterotrimeric G 단백질과 특이적으로 같이 침강하였다. 이러한 결과들은 kinesin-I는 heterotrimeric G 단백질이 포함된 소포를 미세소관을 따라 이동시킴을 시사한다.

• BMB Reports
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• 제45권4호
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• pp.239-241
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• 2012

Iron availability is limited in the environment and most bacteria have developed a system to acquire iron from host hemoproteins. Heme oxygenase plays an important role by degrading heme group and releasing the essential nutrient iron. The structure of Bacillus subtilis HmoB was determined to 2.0 ${\AA}$ resolution. B. subtilis HmoB contains a typical antibiotic biosynthesis monooxygenase (ABM) domain that spans from 71 to 146 residues and belongs to the IsdG family heme oxygenases. Comparison of HmoB and IsdG family proteins showed that the C-terminal region of HmoB has similar sequence and structure to IsdG family proteins and contains conserved critical residues for heme degradation. However, HmoB is distinct from other IsdG family proteins in that HmoB is about 60 amino acids longer in the N-terminus and does not form a dimer whereas previously studied IsdG family heme oxygenases form functional homodimers. Interestingly, the structure of monomeric HmoB resembles the dimeric structure of IsdG family proteins. Hence, B. subtilis HmoB is a heme oxygenase with a novel structural feature.

• BMB Reports
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• 제34권2호
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• pp.95-101
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• 2001

Tissue transglutaminase (TGII, $G{\alpha}h$) belongs to a family of enzymes which catalyze post-translational modification of proteins by forming isopeptides via $Ca^{2+}$-dependent reaction. Although TGII-mediated formation of isopeptides has been implicated to play a role in a variety of cellular processes, the physiological function of TGII remains unclear. In addition to this Tease activity, TGII is a guanosine triphosphatase (GTPase) which binds and hydrolyzes GTP It is now well recognized that the GTPase action of TGII regulates a receptor-mediated transmembrane signaling, functioning as a signal transducer of the receptor. This TGII function signifies that TGII is a new class of GTP-binding regulatory protein (G-protein) that differs from "Classical" heterotrimeric G-proteins. Regulation of enzyme is an important biological process for maintaining cell integrity. This review summarizes the recent development in regulation of TGII that may help for the better understanding of this unique enzyme. Since activation and inactivation of GTPase of TGII are similar to the heterotrimeric G-proteins, the regulation of heterotrimeric G-protein in the transmembrane signaling is also discussed.

• BMB Reports
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• 제33권6호
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• pp.440-447
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• 2000

In this study HepG2 cells were used to express and purify HBV pol proteins. In order to facilitate purification of HBV pol proteins, HBV pol and its deletion mutants were fused to MBP (Maltose Binding Protein). As a result we successfully expressed and partially purified both wild type and mutant recombinant HBV pol proteins by using an amylose resin and anti-MBP antibody. In the case of wild type, the anti-MBP antibody detected three bands. One was full-length and the others were generated by proteolysis of the terminal domain region. The expressed MBP/POL proteins were localized both in the cytoplasm and in the perinuclear region. The purified proteins had polymerase activity toward an exogenous homo-polymer template. The MBP/POL protein also had DNA synthesis activity in vivo, since the MBP/POL expression construct was able to complement a HBV polymerase mutant in trans.

• 미생물학회지
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• 제31권2호
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• pp.166-174
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• 1993

Streptomyces coelicolor (Muller) 의 세포에 $100 \mu$M 의 과산화수소를 1시간 동안 처리하여 과산화수소 스트레스중에 생성되는 단백질을 L-[$^{35}S$] methionine 을 이용하여 순간 표지하였다. 단백질을 추출하여 2차원 겔 전기영동으로 분석한 결과 지수 성장기의 세포가 가지는 총세포 단백질 중 약 100개의 단백질의 합성이 과산화수소에 의해 증가되는 것을 관찰하였다. 이들을 Pin(peroxide inducible) 단백질이라고 명명하고 과상화수소 처리 후 발현이 증가되는 시간에 따라 세 그룹으로 나누었다. 약 60 개의 Pin 단백질은 과산화수소 처리후 20분 이내에 발현이 증가하여 1시간동안 지속적으로 다량 합성되었다. 정체 성장기의 세포에서는 62개의 단백질의 합성이 과산화수소에 의해 증가되었으며, 이 중 21 개의 단백질은 지수성장기의 Pin 단백질과 일치하였다. 과산화수소에 대한 저항성이 증가한 세가지 돌연변이체의 단백질을 지수 성장기에서 추출하여 2 차원 겔 전기영동으로 분석한 결과, 각각의 경우 15, 17, 15개의 Pin 단백질을 야생형보다 항상적으로 다량합성하는 것을 관찰하였다. 이 pin 단백질 중 9개 (D74.7 a, E76.0c, E23.3, F50.7, F47.2a, F25.5, G39.6b, G24.0, H39.6a) 는 두가지 돌연변이체 모두에게 증가되었다. 따라서 이 단백질들은 S. coelicolor 가 과산화수소 스트레스에 대응하는데 있어 중요한 역할을 담당한다고 추정된다.

• Journal of Microbiology
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• 제44권2호
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• pp.145-154
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• 2006

Heterotrimeric G proteins (G proteins) are conserved in all eukaryotes and are crucial components sensing and relaying external cues into the cells to elicit appropriate physiological and biochemical responses. Basic units of the heterotrimeric G protein signaling system include a G protein-coupled receptor (GPCR), a G protein composed of ${\alpha},\;{\beta},\;and\;{\gamma}$ subunits, and variety of effectors. Sequential sensitization and activation of these G protein elements translates external signals into gene expression changes, resulting in appropriate cellular behaviors. Regulators of G protein signaling (RGSs) constitute a crucial element of appropriate control of the intensity and duration of G protein signaling. For the past decade, G protein signaling and its regulation have been intensively studied in a number of model and/or pathogenic fungi and outcomes of the studies provided better understanding on the upstream regulation of vegetative growth, mating, development, virulence/pathogenicity establishment, and biosynthesis of secondary metabolites in fungi. This review focuses on the characteristics of the basic upstream G protein components and RGS proteins, and their roles controlling various aspects of biological processes in the model filamentous ascomycete fungus Aspergillus nidulans. In particular, their functions in controlling hyphal proliferation, asexual spore formation, sexual fruiting, and the mycotoxin sterigmatocystin production are discussed.