• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2003.05a
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• pp.221-222
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• 2003

Typically, closed production system units are subject to an accumulation of fine suspended solids and dissolved organics (Weeks et at., 1992). Foam fractionation process is believed to be most effective in marine application for solids removal. In present experiment, the performance of foam fractionator for removal of solids, protein, and other dissolved materials was evaluated at different foam overflow heights and air flow rates in a pilot-scale recirculating aquaculture system for culture of Korean rockfish. (omitted)

• Journal of Microbiology and Biotechnology
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• v.19 no.7
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• pp.727-733
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• 2009

Heat shock protein 70 kDa (hsp70), a molecular chaperone involved in folding of nascent proteins, has been studied for its ability to activate innate and specific immunity. High purity hsp70 preparation is generally required for immunization experiments, because endotoxins and other immunologically active contaminants may affect immune responses independently of hsp70. We have developed a novel modification of E. coli-expression medium that enabled a simple two-step production and purification method for endotoxin-free recombinant hsp70. During Ni-NTA-based affinity purification of hsp70, a contaminating protein from host E. coli cells, L-glutamine-n-fructose-6-phosphate aminotransferase (GFAT), was identified. By testing various compounds, supplementation of growth medium with a GFAT metabolite,N-acetylglucosamine, was found to reduce GFAT expression and increase the total hsp70 yield five times. The new protocol is based on column purification of His-tagged hsp70 protein produced by E. coli with the modified medium, followed by endotoxin removal by Triton X-114 extraction. This approach yielded hsp70 with high purity and minimal endotoxin contamination, making the final product acceptable for immunization experiments. In summary, a simple modification of growth medium allowed production of recombinant mouse hsp70 in high yield and purity, thus compatible with immunological studies. This protocol may be useful for production of other Histagged proteins expressed in E. coli.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2003.10a
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• pp.26-51
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• 2003

Large scale protein interaction maps provide a new, global perspective with which to analyse protein function. PSIMAP, the Protein Structural Interactome Map, is a database of all the structurally observed interactions between superfamilies of protein domains with known three-dimensional structure in thePDB. PSIMAP incorporates both functional and evolutionary information into a single network. It makes it possible to age protein domains in terms of taxonomic diversity, interaction and function. One consequence of it is to predict the most important protein domain structure in evolution. We present a global analysis of PSIMAP using several distinct network measures relating to centrality, interactivity, fault-tolerance, and taxonomic diversity. We found the following results: ${\bullet}$ Centrality: we show that the center and barycenter of PSIMAP do not coincide, and that the superfamilies forming the barycenter relate to very general functions, while those constituting the center relate to enzymatic activity. ${\bullet}$ Interactivity: we identify the P-loop and immunoglobulin superfamilies as the most highly interactive. We successfully use connectivity and cluster index, which characterise the connectivity of a superfamily's neighbourhood, to discover superfamilies of complex I and II. This is particularly significant as the structure of complex I is not yet solved. ${\bullet}$ Taxonomic diversity: we found that highly interactive superfamilies are in general taxonomically very diverse and are thus amongst the oldest. This led to the prediction of the oldest and most important protein domain in evolution of lift. ${\bullet}$ Fault-tolerance: we found that the network is very robust as for the majority of superfamilies removal from the network will not break up the network. Overall, we can single out the P-loop containing nucleotide triphosphate hydrolases superfamily as it is the most highly connected and has the highest taxonomic diversity. In addition, this superfamily has the highest interaction rank, is the barycenter of the network (it has the shortest average path to every other superfamily in the network), and is an articulation vertex, whose removal will disconnect the network. More generally, we conclude that the graph-theoretic and taxonomic analysis of PSIMAP is an important step towards the understanding of protein function and could be an important tool for tracing the evolution of life at the molecular level.

• Clean Technology
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• v.6 no.1
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• pp.71-78
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• 2000

Removal rates of hydrogen sulfide were investigated to known effects of several light sources with external and internal irradiation on the desulfurization using C. thiosulfatophilum. In the case of internal illumination system, optical-fiber photobioreactor was applied to increase the light availability. Furthermore, sunlight was used as the main light energy in the daytime and metal-halide lamp was applied as an additional light energy at night. Light energy of 99% was saved by the application of the LED's array in comparison with the incandescent light source. $H_2S$ removal rates at 5,000 lux in a 4-L photobioreactor were shown as 0.040, 0.138, 0.136, and 0.134 (${\mu}mol$ $H_2S/min$)/(mg protein/L), respectively, in the following order of light sources, when several light sources such as fluorescent, energy-saving, incandescent, halogen lamp, and filtered light at 460 nm were applied. Removal rate per unit cell concentration with the internal light diffused optical-fibers increased about 1 six times as much as that with the external light sources. Removal rate per unit cell concentration, using sunlight in the daytime and a metal-halide lamp at night, was 0.41 less than 0.869 (${\mu}mol$ $H_2S/min$)/(mg protein/L) using a 400 W metal-halide lamp day and night, since the automatic sunlight collection system can transmit the light intensity as only 10% of that with a metal-halide lamp.

• Journal of Photoscience
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• v.9 no.2
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• pp.55-58
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• 2002

The reaction center Dl protein of photosystem II is the target of photodamage by excess illumination. The Dl protein is damaged by reactive oxygen species generated by photochemical reactions and then degraded by specific proteolytic enzymes. We found that the Dl protein also cross-links with the surrounding polypeptides, such as D2 and CP43 in isolated thylakoids or photosystem II-enriched membranes from spinach under the illumination with strong visible light. The cross-linking was observed in spinach leaf discs as well when they were illuminated at higher temperature (40°C). It was also shown that the cross-linked products are digested efficiently by a protease(s) in the stroma. Thus the cross-linking/digestion processes of the Dl protein seem to comprise a new pathway in the turnover of the photodamaged Dl protein. It should be noted, however, that the cross-linked products of the Dl protein and CP43 induced by endogenous cationic radicals in the donor-side photoinhibition are resistant to proteolytic digestion. Accumulation of these cross-linked products in the thylakoids may lead to the decay of the function of chloroplasts and finally to the death of plant cells. Thus, we suggest that the quality control of photosystem II, especially removal of the cross-linked products of the Dl protein, is crucial for the survival of chloroplasts under the light stress.

• KOREAN JOURNAL OF CROP SCIENCE
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• v.38 no.2
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• pp.159-165
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• 1993

To clarify the effects of sink demand for assimilate on leaf photosynthetic rate, tissue composition, and leaf senescence of soybean [Glycine max (L.) Merr.] J plants, pod and leaf tissues were removed at growth stage $R^3$. Plant responses were measured every 10days from 2 through 42days following treatment. Leaves of depodded plants exhibited increased starch and chlorophyll contents and specific leaf weight. Stomatal resistance was also increased and leaf photosynthetic rate was reduced. Dry weight of vegetative tissues except leaves was increased by pod removal. Leaf removal resulted in a decreased starch content of leaves from 22 to 42days after treatment and that of roots at all sampling times. Specific leaf weight was decreased while leaf photosynthetic rate was increased. Stomatal resistance and chlorophyll content were little affected. Weight per seed was decreased 3.0% by leaf removal. Except for the seed, tissue protein contents were increased by pod removal but decreased by leaf removal, however, seed protein content was not affected by either. Apparent senescence was delayed by depodding. Both apparent and functional senescence were accelerated by leaf removal.

• BMB Reports
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• v.49 no.9
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• pp.459-473
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• 2016

Neurodegenerative diseases (NDs) often involve the formation of abnormal and toxic protein aggregates, which are thought to be the primary factor in ND occurrence and progression. Aged neurons exhibit marked increases in aggregated protein levels, which can lead to increased cell death in specific brain regions. As no specific drugs/therapies for treating the symptoms or/and progression of NDs are available, obtaining a complete understanding of the mechanism underlying the formation of protein aggregates is needed for designing a novel and efficient removal strategy. Intracellular proteolysis generally involves either the lysosomal or ubiquitin-proteasome system. In this review, we focus on the structure and assembly of the proteasome, proteasome-mediated protein degradation, and the multiple dynamic regulatory mechanisms governing proteasome activity. We also discuss the plausibility of the correlation between changes in proteasome activity and the occurrence of NDs.

• Korean Journal of Fisheries and Aquatic Sciences
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• v.36 no.5
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• pp.509-514
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• 2003

We performed the experiment to determine the effective factors, such as the initial concentration of protein, pore size of air distributor, SAV (superficial air velocity), pH, salts and temperature related to foaming characteristics. The foam height in a foam generator was increased with the increase of the initial protein concentration and the decrease of pore size. As SAV was increased, the foam height was increased, and the optimum SAV was 0.84 cm/sec. The foam height was highest in the acid region and it was increased with the increase of salt concentration of NaCl and $NaHCO_3.$ The removal efficiencies of TSS (total suspended solid) and turbidity decreased with the increase of the initial protein concentration in the batch foam separator.

• Journal of Applied Biological Chemistry
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• v.42 no.2
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• pp.81-84
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• 1999

Blood glue was prepared to reutilize porcine blood. Plasma proteins after lyophilization were treated by addition of wood flour, sodium hydroxide, sodium silicate, and hydrated lime to make blood glue with a suitable adhesivity. Characteristics of the prepared blood glue was monitored by measuring the viscosity with time, and the relationship between degree of hydrolysis of plasma proteins by addition of various amounts of sodium hydroxide and adhesivity was studied. To prevent the emission of formaldehyde during manufacturing of plywood by blood glue, the cross-linking reaction of plasma protein with formaldehyde was also examined. Fourier transform infrared, circular dichroism, and fluorescence spectroscopy study showed that blood plasma proteins react with formaldehyde, resulting in removal of formaldehyde by cross-linking reaction.

• Biotechnology and Bioprocess Engineering:BBE
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• v.3 no.2
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• pp.82-86
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• 1998

The maltose binding protein (MBP) fusion protein system is a versatile tool to express and isolate recombinant proteins in E. coli. In this system, MBP fusion proteins are efficiently isolated from whole cell lysate using amylose conjugated agarose beads and then eluted by competition with free maltose. Since MBP is a rather large molecule (∼42 kDa), for further experiments, the MBP part is usually proteolytically cleaved from the fusion protein and subsequently removed by ion-exchange chromatography or rebinding to amylose columns after washing out excess and MBP-bound maltose. In the present study, we have developed an improved method for the removal of cleaved MBP, which is advantageous over conventional methods. In this method, factor Xa cleaved MBP fusion proteins were incubated with Sepharose beads conjugated with MBP specific monoclonal antibodies and then precipitated buy centrifugation, resulting in highly purified proteins in the supernatant.