• Title, Summary, Keyword: Proteins

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도축 폐혈액 단백질을 이용한 유산균체의 생산

  • 현창기;신현길
    • Microbiology and Biotechnology Letters
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    • v.25 no.2
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    • pp.218-223
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    • 1997
  • For the utilization of animal blood produced in slaughter for the cultivation of lactic acid bacteria, the nitrogen sources in a complex(MRS) medium were replaced by blood plasma proteins. Focusing the purpose on the industrial production of a probiotics, the hydrolytic activities of three industrially applicable proteases were compared for the effective digestion of the proteins, and Alcalase(the product of Novo Nordisk) was selected with comparatively high activity. The growth of Streptococcus thermophilus KCCM12020 was best among the four strains of lactic acid bacteria tested. With Alcalase-digested proteins in the medium, the growth rates and the final cell concentrations were higher than those with non-digested proteins. The cell mass produced in the medium containing blood proteins as nitrogen sources, $2.5{\times}10^9$ CFU/ml, was significantly high and about 70% of that in MRS medium, showing a great possibility for the utilization of animal blood proteins as economic nitrogen sources in the production of cell mass of lactic acid bacteria.

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Effects of Bambusae Caulis in Liquamen on the Stress Proteins Induced by Heating in Endothelial Cells (혈관내피세포에 열 충격 부과시 죽력이 stress proteins의 발현에 미치는 영향)

  • Jeon Hoon
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.18 no.2
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    • pp.496-499
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    • 2004
  • We have previously observed that Bambusae Caul is in Liquamen (BCL) stimulates the adipose conversion of 3T3-L1 cells and molecular chaperones were involved in the process of the assembly and replacement of laminin subunits in Bovine aortic endothelial cells(BAEC). Endothelial cells are exposed to continuous shear stress due to the blood flow. Heat shock protens(hsp) are a well-known stress response protein, namely, stress proteins. To investigate effects of BCL on the stress proteins induced by heating in endothelial cells, we have analyzed synthetic amounts of stress proteins in sodium dodecyl sulfate gel electrophoresis under reducing conditions. Under the condition of heating stress, BCL inhibited the synthesis of stress proteins in endothelial cells. These results suggest that BCL may have an important role for expression of stress proteins induced by heating in endothelial cells.

Heat Shock Proteins: A Review of the Molecular Chaperones for Plant Immunity

  • Park, Chang-Jin;Seo, Young-Su
    • The Plant Pathology Journal
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    • v.31 no.4
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    • pp.323-333
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    • 2015
  • As sessile organisms, plants are exposed to persistently changing stresses and have to be able to interpret and respond to them. The stresses, drought, salinity, chemicals, cold and hot temperatures, and various pathogen attacks have interconnected effects on plants, resulting in the disruption of protein homeostasis. Maintenance of proteins in their functional native conformations and preventing aggregation of non-native proteins are important for cell survival under stress. Heat shock proteins (HSPs) functioning as molecular chaperones are the key components responsible for protein folding, assembly, translocation, and degradation under stress conditions and in many normal cellular processes. Plants respond to pathogen invasion using two different innate immune responses mediated by pattern recognition receptors (PRRs) or resistance (R) proteins. HSPs play an indispensable role as molecular chaperones in the quality control of plasma membrane-resident PRRs and intracellular R proteins against potential invaders. Here, we specifically discuss the functional involvement of cytosolic and endoplasmic reticulum (ER) HSPs/chaperones in plant immunity to obtain an integrated understanding of the immune responses in plant cells.

Screening Molecular Chaperones Similar to Small Heat Shock Proteins in Schizosaccharomyces pombe

  • Han, Jiyoung;Kim, Kanghwa;Lee, Songmi
    • Mycobiology
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    • v.43 no.3
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    • pp.272-279
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    • 2015
  • To screen molecular chaperones similar to small heat shock proteins (sHsps), but without ${\alpha}$-crystalline domain, heat-stable proteins from Schizosaccharomyces pombe were analyzed by 2-dimensional electrophoresis and matrix assisted laser desorption/ionization time-of-flight mass spectrometry. Sixteen proteins were identified, and four recombinant proteins, including cofilin, NTF2, pyridoxin biosynthesis protein (Snz1) and Wos2 that has an ${\alpha}$-crystalline domain, were purified. Among these proteins, only Snz1 showed the anti-aggregation activity against thermal denaturation of citrate synthase. However, pre-heating of NTF2 and Wos2 at $70^{\circ}C$ for 30 min, efficiently prevented thermal aggregation of citrate synthase. These results indicate that Snz1 and NTF2 possess molecular chaperone activity similar to sHsps, even though there is no ${\alpha}$-crystalline domain in their sequences.

Roles of Sperm Proteins

  • Cho, Chung-Hee
    • 대한생식의학회:학술대회논문집
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    • pp.57-62
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    • 2001
  • One of recent advances of mammalian fertilization is the understanding of the molecular basis of fertilization. Several proteins localized in sperm nucleus or on sperm surface are necessary for the fertilization process. Protamines, sperm nuclear proteins, are required for normal sperm function that leads to fertilization. Fertilin and cyritestin are sperm surface proteins and essential for sperm-egg binding. Fertilin is also required for sperm transport in the female reproductive tracts. Metalloproteses on sperm plasma membrane are found to play a role in sperm-egg fusion. The functional analysis of these proteins provides a new insight into the molecular mechanisms underlying mammalian fertilization and male fertility.

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Immunoblot findings of calcareous corpuscles binding proteins in cyst fluid of Taenia solium metacestodes

  • Yang, Hyun-Jong
    • The Korean Journal of Parasitology
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    • v.42 no.3
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    • pp.141-143
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    • 2004
  • After collecting calcareous corpuscles from plerocercoid of Spirometra mansoni (sparganum), we evaluated the antigenic values of calcareous corpuscles binding proteins obtained from the cyst fluid of Taenia solium metacestodes. Immunoblot analysis revealed that cysticercosis patient sera strongly recognized 10 and 95 kDa calcareous corpuscles binding proteins. This result demonstrated that calcareous corpuscles are bound with major secretory antigenic proteins, which is possibly involved in the secretory pathways of the 10 and 95 kDa proteins presenting in the cyst fluid of T. solium metacestodes.

Comparison of Protein-Protein Interaction from Geometry and Biochemistry View with Computation-Driven Data

  • Devi D/O S, Shree Sundari;Keong, Kwoh-Chee;Kolatkar, Prasanna R
    • Proceedings of the Korean Society for Bioinformatics Conference
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    • pp.402-406
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    • 2005
  • In this paper, we present a tool to calculate the distribution of amino acid contacts in proteins as well as in protein domains. The proteins are grouped according to the classification by Yanay Ofran and Burkhard Rost[1]. In addition, a protein's distribution was compared with that of proteins in the same group as well as the entire collection of proteins across all groups. With these statistics, biologists can pick out proteins which have characteristics that defer from the norm.

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The Role and Regulation of MCL-1 Proteins in Apoptosis Pathway

  • Bae, Jeehyeon
    • Proceedings of the Korean Society of Applied Pharmacology
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    • pp.113-113
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    • 2002
  • Phylogenetically conserved Bcl-2 family proteins play a pivotal role in the regulation of apoptosis from virus to human. Members of the Bcl-2 family consist of antiapoptotic proteins such as Bcl-2, Bcl-xL, and Bcl-w, and proapoptotic proteins such as BAD, Bax, BOD, and Bok. It has been proposed that anti- and proapoptotic Bcl-2 proteins regulate cell death by binding to each other and forming heterodimers. A delicate balance between anti- and proapoptotic Bcl-2 family members exists in each cell and the relative concentration of these two groups of proteins determines whether the cell survives or undergoes apoptosis. Mcl-1 (Myeloid cell :leukemia-1) is a member of the Bcl-2 family proteins and was originally cloned as a differentiation-induced early gene that was activated in the human myeloblastic leukemia cell line, ML-1 . Mcl-1 is expressed in a wide variety of tissues and cells including neoplastic ones. We recently identified a short splicing variant of Mcl-1 short (Mcl-IS) and designated the known Mcl-1 as Mcl-1 long (Mcl-lL). Mcl-lL protein exhibits antiapoptotic activity and possesses the BH (Bcl-2 homology) 1, BH2, BH3, and transmembrane (TM) domains found in related Bcl-2 proteins. In contrast, Mcl-1 S is a BH3 domain-only proapoptotic protein that heterodimerizes with Mcl-lL. Although both Mc1-lL and Mcl-lS proteins contain BH domains fecund in other Bcl-2 family proteins, they are distinguished by their unusually long N-terminal sequences containing PEST (proline, glutamic acid, serine, and threonine) motifs, four pairs of arginine residues, and alanine- and glycine-rich regions. In addition, the expression pattern of Mcl-1 protein is different from that of Bcl-2 suggesting a unique role (or Mcl-1 in apoptosis regulation. Tankyrasel (TRF1-interacting, ankyrin-related ADP-related polymerasel) was originally isolated based on its binding to TRF 1 (telomeric repeat binding factor-1) and contains the sterile alpha motif (SAM) module, 24 ankyrin (ANK) repeats, and the catalytic domain of poly(adenosine diphosphate-ribose) polymerase (PARP). Previous studies showed that tankyrasel promotes telomere elongation in human cells presumably by inhibiting TRFI though its poly(ADP-ribosyl)action by tankyrasel . In addition, tankyrasel poly(ADP-ribosyl)ates Insulin-responsive amino peptidase (IRAP), a resident protein of GLUT4 vesicles, and insulin stimulates the PARP activity of tankyrase1 through its phosphorylation by mitogen-activated protein kinase (MAPK). ADP-ribosylation is a posttranslational modification that usually results in a loss of protein activity presumably by enhancing protein turnover. However, little information is available regarding the physiological function(s) of tankyrase1 other than as a PARP enzyme. In the present study, we found tankyrasel as a specific-binding protein of Mcl-1 Overexpression of tankyrasel led to the inhibition of both the apoptotic activity of Mel-lS and the survival action of Mcl-lL in mammalian cells. Unlike other known tankyrasel-interacting proteins, tankyrasel did not poly(ADP-ribosyl)ate either of the Mcl-1 proteins despite its ability to decrease Mcl-1 proteins expression following coexpression. Therefore, this study provides a novel mechanism to regulate Mcl-1-modulated apoptosis in which tankyrasel downregulates the expression of Mcl-1 proteins without the involvement of its ADP-ribosylation activity.

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Changes of Binding Ability of Milk-Hypersensitive Patients질 IgE to Gamma-Irradiated Milk Proteins (감마선 조사된 우유단백질에 대한 우유 알러지 환자의 IgE 결합능의 변화)

  • 조경환;육홍선;이주운;이수영;변명우
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.30 no.3
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    • pp.505-509
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    • 2001
  • This study was carried out to evaluate the application of food irradiation technology as a method for reducing milk allergies. Bovine $\alpha$-casein, $\beta$-casein, $textsc{k}$-casein, $\alpha$-lactalbumin(ALA), $\beta$-lactoglobulin (BLG) and serum albumin (BSA) were used as model allergens of milk proteins and the proten solution (2.0 mg/mL) with 0.01 M phosphate buffered saline (pH 7.4) was irradiated at 3, 5 and 10 kGy. Using milk-hypersensitive patients IgE (MHP-IgE), the changes of binding ability to irradiated proteins were observed by competitive indirect enzyme-linked immunosorbent assay (Ci-ELISA). Affinity of MHP-IgE to milk proteins was higher in ALA and BLG than that of other proteins. Standard curve to each non-irradiated protein could be made with MHP-IgE for quantifying milk allergens. Binding abilities of MHP-IgE to the irradiated proteins, however, decreased with different slopes of the standard curves. Sensitivity of gamma irradiation was higher in ALA and BLG than of other proteins. These results indicated that irradiation technology can be used to reduce the milk hypersensitivity.

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Changes of haemolymph proteins in Pieris rapae L. during the cuticle formation and hardening process (배추흰나비의 큐티클 形成과 硬化에 따른 혈림프 단백질의 變化)

  • Hak Ryul Kim;Eul Won Seo
    • The Korean Journal of Zoology
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    • v.23 no.1
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    • pp.1-12
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    • 1980
  • Changes and possible origin of haemolymph proteins during the cuticle formation and hardening are determined by means of acrylamide gel electrophoresis and immunodiffusion. The results by acrylamide gel electrophoresis showed at least 19 protein bands in the haemolymph and 13 fractions in the fat body with relatively constant pattern during the period of cuticle formation and hardening. Both haemolymph and fat body proteins are generally characterized by the presence of three to four heavy stained bands and several thin bands near the top region of the gel. At least over five haemolymph proteins are constantly present during this period. Immunodiffusion tests show that of total eight to nine pupal haemolymph proteins two proteins were already detected in the fat body before pupation and other two proteins were also found in the fat body immediately after pupation, suggesting fat body as possible source of these two haemolymph proteins.

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