• Korean Journal of Food Science and Technology
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• v.16 no.3
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• pp.322-328
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• 1984

These experiments were conducted to purify the glucoamylase produced by Rhizopus oryzae. Two forms of glucoamylase (GI and GII) from Phizopus oryzae were purified by $(NH_2)_2SO_4$ fractionation, acetone fractionation and successive column chromatography on DEAE-cellulose and CM-cellulose. The specific activities of GI and GII toward soluble starch were 157.6 U/㎎. protein (37.5 fold of crude extract), and 164.7 U/㎎. protein (39.2 fold of curde extract), respectively, and the yields of them were 4.3% and 3.8%, respectively. The two purified enzymes have shown a single band by polyacrylamide disc gel electrophoresis and SDS-polyacrylamide gel electrophoresis. The protein bands of their electrophoresis gel were revealed to have glucoamylase activity by iodine staining and were proved to be glycoprotein by periodic acid Schiff's staining.

• Journal of Sericultural and Entomological Science
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• v.28 no.1
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• pp.30-36
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• 1986

Polyacrylamide gel electrophoresis and autoradiography were applied to investigate the developmental profiles of the major hemplymph proteins (MHPs) and their biosynthesis. In addition, some biochemical methods were also used to isolate and purify the MHPs. The obtained results are summarized as follows. 1. MHP-a began to appear from the 2nd day of the fourth-instar larva while MHP-b and -c were detected first on the 1st day of the fifth-instar larva. All these proteins, however, showed a drastic increase in concentration at the 2nd day of the fifth-instar larva. 2. MHP-b and -c were synthesized in fat body on early day of the fifth-instar larva, but the possibility of MHP-a synthesis in fat body was excluded. 3. MHP-b was isolated and purified by heat-treatment (6$0^{\circ}C$), gel filtration on Sephadex G-100 and column chromatography on DEAE-cellulose and CM-cellulose. Purified MHP-b showed a single band on polyacrylamide gel- and SDS-polyacrylamide gel electrophoresis.

• Journal of the Korean Society of Radiology
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• v.83 no.1
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• pp.230-238
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• 2022

Polyacrylamide gel (PAAG) has been used for augmentation mammoplasty in certain countries, such as China or Eastern European countries. However, owing to various complications, its use is currently banned in most countries. Nevertheless, because of the migratory stream of female from these countries, we also encounter patients with PAAG mammoplasty in Korea. Owing to the various imaging features of PAAG mammoplasty, it may interfere with the identification of malignancy or other pathologic conditions. Therefore, it is important to identify the imaging findings related to PAAG mammoplasty. However, there is limited literature on the radiologic findings of complications related to PAAG mammoplasty in Korea. Herein we report four cases of PAAG mammoplasty, the complications faced, and depict various radiologic features through multimodality imaging.

• Environmental Engineering Research
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• v.12 no.1
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• pp.21-29
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• 2007

For this study, we polymerized polyacrylamide base flocculants (PAA) and tested their properties and settling efficiency as a treatment for potable water. The most common chemicals for potable water treatment in Korea are alum or PAC. However, due to various reasons (such as rainy season or algae), inorganic flocculants cannot be solely depended on to solve all the problems caused by the poor quality of inflow water. When PAA coupled with coagulants in a potable water purification process is used, the turbidity removal efficiency increases by a factor of three on a single chemical system using PAC (Raw water: 5.21 NTU; Treated PAA+PAC: 0.34 NTU; and, Treated PAC: 1.04 NTU). It is possible to offset the toxic effect of residual monomers in treated water using PAA, because the concentrations of residual acrylamide are less than 400 mg/L in the polymer itself and less than $0.04\;{\mu}g/L$ in the treated water base at a dosage of 0.1 mg/L. Therefore, PAAs may be a workable, and dependable, potable water treatment process for the high pollutant level of resource water.

• Polymer(Korea)
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• v.39 no.3
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• pp.403-411
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• 2015

A series of hydrophobically associating fluorinated amphiphilic polyacrylamide copolymers with remarkably high heat resistance and salt tolerance were synthesized by free radical micellar copolymerization, using acrylamide (AM) and sodium 2-acrylamido-tetradecane sulfonate ($AMC_{14}S$) as amphiphilic monomers, and 2-(perfluorooctyl) ethyl acrylate (PFHEA) as hydrophobic monomer. The structure of the terpolymer was characterized by FTIR, $^1H$ NMR and $^{19}F$ NMR. The solution properties of the terpolymers were investigated in details, and the results showed that the terpolymer solution had strong intermolecular hydrophobic association as the concentration exceeded the critical association concentration 1.5 g/L. The terpolymer solution possessed high surface activity, viscoelasticity, excellent heat resistance, salt tolerance and shearing resistance. The viscosity retention rate of copolymer solution was as high as 59.9% under the condition of fresh wastewater, $85^{\circ}C$ and a 60-days aging test.

• Journal of Microbiology and Biotechnology
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• v.9 no.4
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• pp.482-487
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• 1999

The Pseudomonas sp. strain NGK1 (NCIM 5120) was immobilized in calcium alginate, agar, and polyacrylamide gel matrices. The salicylic acid-producing capacity of freely suspended cells was compared with immobilized cells in batches with a shake culture and continuous culture system in a packed bed reactor. Freely suspended cells ($4\times10^{10}cfu/ml$) produced 12 mM of salicylic acid, whereas cells immobilized in calcium alginate ($1.8\times10^{11}$cfu/g beads), agar ($1.8\times10^{11}$cfu/g beads), and polyacrylamide ($1.6\times10^{11}$cfu/g beads) produced 15, 11, and 16mM of salicylic acid, respectively, from naphthalene at an initial concentration of 25 mM. The continuous production of salicylic acid from naphthalene was investigated in a continuous packed bed reactor with two different cell populations. The longevity of the salicylic acid-producing activity of the immobilized cells from naphthalene was also studied in semi continuous fermentations. The immobilized cells could be reused 18, 13, and more than 20 times without losing salicylic acid-producing activity in calcium alginate-,agar-, and polyacrylamide-entrapped cells, respectively. The study reveals a more efficient utilization of naphthalene and salicylic acid production by the immobilized Pseudomonas sp. strain NGK1 as compared to the free cells.

• The Korean Journal of Mycology
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• v.18 no.2
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• pp.84-88
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• 1990

Hydroxylation in the $11{\alpha}$-position of progesterone molecules was carried out using Rhizopus nigricans spores immobilized within various gel matrices, among which polyacrylamide and agar gel were proved to be the most effective. Reactions with the immobilized cells and in­tact free cells showed almost identical conversion rate of progesterone, optimal pH and reaction time for attaining maximal yield, from which were confirmed absence of any decay and modification of enzyme activities.

• The Korean Journal of Mycology
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• v.8 no.3
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• pp.159-166
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• 1980

Aspergillus niger van Tieghem was cultured by the method of submerged and synchronized culture for the study of differentiation. Acid-phenol soluble cell proteins of the fungus were extracted from four stages during development. Those acid-phenol soluble proteins were separated by polyacrylamide gel electrophoresis to determine the protein patterns. A new protein band was observed from the pre-sporulation body, color density of the stained protein bands in four tubes differed according to the differentiation stages. The number of protein bands in 10% gels varied from 18 to 16, 17, and 19 according to the course of spore germination stage, conidiophore stage, phialide maturation stage and sporulation stage.

• BMB Reports
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• v.39 no.6
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• pp.717-721
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• 2006

In vitro analyses of type I signal peptidase activities require protein precursors as substrates. Usually, these pre-proteins are expressed in vitro and cleavage of the signal sequence is followed by SDS polyacrylamide gel electrophoresis coupled with autoradiography. Radioactive amino acids have to be incorporated in the expressed protein, since the amount of the in vitro expressed protein is usually very low and processing of the signal peptide cannot be followed by SDS polyacrylamide gel electrophoresis alone. Here we describe a rapid and simple method to express large amounts of a protein precursor in E. coli. We have analyzed the effect of ionophors as well as of azide on the accumulation of expressed protein precursors. Azide blocks the function of SecA and the ionophors dissipate the electrochemical gradient across the cytoplasmic membrane of E. coli. Addition of azide ions resulted in the formation of inclusion bodies, highly enriched with pre-apo-plastocyanine. Plastocyanine is a soluble copper protein, which can be found in the periplasmic space of cyanobacteria as well as in the thylakoid lumen of cyanobacteria and chloroplasts, and the pre-protein contains a cleavable signal sequence at its N-terminus. After purification of cyanobacterial pre-apo-plastocyanine, its signal sequence can be cleaved off by the E. coli signal peptidase, and protein processing was followed on Coomassie stained SDS polyacrylamide gels. We are optimistic that the presented method can be further developed and applied.

• Journal of Microbiology and Biotechnology
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• v.1 no.2
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• pp.90-95
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• 1991

A ${\alpha}-galactosidase{\;}({\alpha}-D-galactoside$ galactohydrolase; EC 3.2.1.22) was purified from the culture filtrate of Penicillium purpurogenum by DEAE-cellulose column chromatography, gel filtration of Bio gel p-l00, and subsequent SP-Sephadex C-25 chromatography. The final preparation thus obtained showed a single band on polyacrylamide disc-gel and SDS-polyacrylamide gel electrophoresis. The molecular weight and isoelectric point were determined to be 63,000 and pH 4.0 by SDS-polyacrylamide gel electrophoresis and isoelectric focusing, respectively. The galactosidase exhibited maximum activity at pH 4.5 and $55^{\circ}C$, and was stable between pH 2 and 5, and also stable up to $40^{\circ}C$. The enzyme activity was not affected considerably by treatment with other metal compounds except mercuric chloride and silver nitrate. Copra galactomannan was finally hydrolyzed to galactose, mannose and mannobiose through the sequential actions of the purified galactosidase and mannanase from the same strain. The enzyme hydrolyzed melibiose and raffinose, but not lactose.