• Title/Summary/Keyword: polyacrylamide,

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PCR-based genotyping of Korean population for forensic applications

  • Ryu, Jae-Song;Gu, Yun-Mo;So, Jae-Seong
    • 한국생물공학회:학술대회논문집
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    • 2000.04a
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    • pp.592-595
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    • 2000
  • In human chromosome, a short sequence of DNA has been repeated a number of times. These repeats are called variable number of tandem repeat(VNTR) or short tandem repeat(STR) which has short repeat core. VNTR and STR are used in the field of forensic science, evolution, and anthropology. In this work, we examined allele frequencies of 3 VNTR(YNZ22, NeuR, D21S11) and one STR(Humth01) in a Korean population sample by polymerase chain reaction(PCR) followed by high-resolution polyacrylamide gelelectrophoresis(PAGE) with silver staining. Subsequently, the polymorphism information content(PIC) was calculated : the highest PIC was observed for the NeuR locus(0.95680) and lowest for the Humth01 locus(0.75809).

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Characterization and Purification of Agarase from Cytophaga sp. ACLJ-18 (한천 분해균(Cytohaga sp. ACLJ-18)이 생산하는 agarase의 정제 및 특성)

  • 주동식;송해미;이정석;조순영;이응호
    • KSBB Journal
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    • v.13 no.3
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    • pp.320-324
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    • 1998
  • Agar degrading enzyme-agarase-was purified from the culture fluid of Cytophaga so/ ACLJ-18, by acetone precipitation, DEAE-Cellulose, Sephadex G-100 and CM-Sephadex C25 column chromatographies. The molecular weight of purified agarase was estimated to be 24,700 dalton by SDS-polyacrylamide gel electrophoresis. The optimum pH and temperature for agarase activity were 7.0 and 40$^{\circ}C$, respectively. this agarase was stable in the pH range of 6.5 - 8.0 and 40$^{\circ}C$, and required 0.35M NaCl for optimum activity. And this agarase was inhibited by metal ions such as Ba2+, Cu2+, Co2+, Mn2+, Hg2+, Zn2+, and showed specificity on agar.

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Purification of Mold Protease Isolated from Katsuobushi (Katsuobushi에서 분리한 곰팡이 protease 분리정제)

  • Kim, Kwan-Woo;Yun, Tai-Uk;Kim, Jun-Pyong
    • Korean Journal of Food Science and Technology
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    • v.23 no.4
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    • pp.394-399
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    • 1991
  • The strain OK-63 isolated from katsuobushi was cultured on wheat bran medium and the isolate was morphologically identified as an Aspergillus niger group and showed maximum pretense activity and multiplication after 6 days of cultivation. Protease was purified by ammonium sulfate fractionation. Sephadex G-100 gel filtration and DEAE-cellulose column chromatography. The purified enzyme showed single band by polyacrylamide gel electrophoresis and the purity was 150 times higer than crude enzyme. The recovery of enzyme activity was found to be 45%.

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Partial Purification of Mussel Adhesive Protein for Mytilus Edulis and Preparation of Mussel Protein Hydrolysates

  • Sun, Nam-Kyu;Song, Kyung-Bin
    • Preventive Nutrition and Food Science
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    • v.5 no.3
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    • pp.148-152
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    • 2000
  • Mussel adhesive protein (MAP) was extracted from Korean Mytilus edulis and then partially purified using Sephacryl S-300 gel permeation chromatography and reversed-phase high performance liquid chromatography. As an indicator of adhesiveness, is 3,4-dihydroxyphenylalanine (DOPA) content was determined. Its DOPA/protein ratio of 0.19 was higher than those of other reports, indicating a good adhesive. The partially purified MAP was confirmed by acid-urea polyacrylamide gel electrophoresis using cetylpiridinium bromide as a cationic detergent. Sea mussel hydrolysates were prepared using three commercial proteases to provide value-added functional materials and their angiotensin converting enzyme (ACE) inhibitory activities were determined. Among hydrolysates of sea mussel, Protamex was the best and further purification would improved ACE inhibitory activity.

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A Study of Polymorphisms of Proline-Rich Protein in the Korean Population (한국인 이하선 타액 내 Proline-rich Protein의 다형현상에 대한 연구)

  • YS Koo;CY Kim
    • Journal of Oral Medicine and Pain
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    • v.13 no.1
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    • pp.35-41
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    • 1988
  • After Akline slab polyacrylamide gel electrophoresis and 3-3' DMB staining of parotid saliva from 100 Korean population, Author have got following conclusions. 1. The gene frequencies of proline-rich protein in the Korean population were Pr1=0.79, Pr2=0.21 2. The gene frequencies of Double-band protein in the Korean population were DB+=0.007, Db-=0.933 3. The gene frequencies of proline-rich protein and Double-band protein of the Korean population were between those of he Chinese and Japanese population.

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Characterization of 1,4-Benzoquinone Reductase from Bovine Liver

  • Kim, Kyungsoon
    • Biotechnology and Bioprocess Engineering:BBE
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    • v.7 no.4
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    • pp.216-220
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    • 2002
  • 1,4-Benzoquinone reductase was purified to electrophoretic homogeneity from bovine liver, and the purified enzyme found to have a molecular mass of 29 kDa, as determined by sodium dodecyl sulfate- polyacrylamide gel electrophoresis The enzyme exhibited pH optimum between 8.0 and 8.5. The apparent fm for 1,4-benzoqulnone was 1.643 mM, and the apparent Km for NADH was 1.837 mM. Various divalent cations, such as Hg$\^$2+/, Cu$\^$2+/, and Zn$\^$2+/, exhibited strong inhibitory effects. The enzyme activity was also strongly inhibited by quercetin, dicumarol, and benzoic acid. Incubation of the enzyme with N-bromosuccinimide and pyridoxal 5’-phosphate led to inhibitions of 100% and 99%, respectively. Accordingly, these results suggest that trypto-phan and Iysine residues are Involved at or near the active sites of the enzyme.

Production of Nuclease Activity in U937 Cells by Phorbol 12-Myristate 13-Acetate and Lipopolysaccharide

  • Kwon, Hyung-Joo;Kim, Doo-Sik
    • BMB Reports
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    • v.36 no.5
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    • pp.520-523
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    • 2003
  • The proliferation and differentiation signals of myelogeneous U937 cells are provided by extracellular stimuli, such as lipopolysaccharide (LPS) and phorbol 12-myristate 13-acetate (PMA). In a DNA-native-polyacrylamide gel assay system, we demonstrated that a particular nuclease activity is expressed in PMA-stimulated U937 cells and secreted into the culture medium. The nuclease activity was induced in U937 cells by LPS treatment, while the secretion of the enzyme was undetected in the culture medium. Therefore, it is likely that the expression and secretion of the particular nuclease in U937 cells are controlled by extracellular stimulations, such as PMA and LPS treatment.

Analysis of Placental Proteins in Somatic Cell Clone Recipient Cows

  • Woo, Jei-Hyun;Chung, Hak-Jae;Kim, Bong-Ki;Ko, Yeoung-Gyu;Kim, Jeom-Soon;Jung, Jin-Kwan;Chang, Won-Kyong
    • Proceedings of the KSAR Conference
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    • 2004.06a
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    • pp.197-197
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    • 2004
  • The purpose of this experiment was to investigate the protein profiles in the placenta of Korean native cows(KNC) transferred cloned embryos and KNC artificially inseminated placental tissues were collected from the cows after cesarean section around parturition, and placental proteins were analyzed. Using two dimensional polyacrylamide gel eletrophoresis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. (omitted)

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Purification and Characterization of Inulin Fructotransferase (Depolymerizing) from Arthrobacter sp. A-6

  • PARK, JEONG-BOK;YONG-JIN CHOI
    • Journal of Microbiology and Biotechnology
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    • v.6 no.6
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    • pp.402-406
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    • 1996
  • Inulin fructotransferase (depolymerizing) (EC 2.4.1.93) was purified 34-fold from the culture broth of Arthrobacter sp. A-6 by using a combination of ammonium sulfate fractionation, DEAE-Sepharose CL-6B chromatography and Sephacryl S-200 gel filtration. The purified enzyme converts inulin into di-D-fructofuranose dianhydride III(DFA III) and small quantities of fructo-oligosaccharides. The temperature and pH optima of the enzyme were $70^{\circ}C$ and 6.0, respectively. Molecular weight of the enzyme was determined to be 49 kDa by 12$%$ SDS-polyacrylamide gel electrophoresis, and 145 kDa by Sephacryl S-200gel filtration. This indicates that the functional inulin fructotransferase of Arthrobacter sp. A-6 has a homomeric trimer structure. The enzyme had an isoelectric point of pH 4.6. The N-terminal amino acid sequence of the purified enzyme subunit was Ala-Asp-Asn-Pro-Asp-Gly(\ulcorner)-Ser-Asn-Met(or Glu)-Tyr-Asp-Val.

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Purification and Biochemical Properties of Glutathione S-Transferase from Lactuca sativa

  • Park, Hee-Joong;Cho, Hyun-Young;Kong, Kwang-Hoon
    • BMB Reports
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    • v.38 no.2
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    • pp.232-237
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    • 2005
  • A glutathione S-transferase (GST) from Lactuca sativa was purified to electrophoretic homogeneity approximately 403-fold with a 9.6% activity yield by DEAE-Sephacel and glutathione (GSH)-Sepharose column chromatography. The molecular weight of the enzyme was determined to be approximately 23,000 by SDS-polyacrylamide gel electrophoresis and 48,000 by gel chromatography, indicating a homodimeric structure. The activity of the enzyme was significantly inhibited by S-hexylGSH and S-(2,4-dinitrophenyl) glutathione. The enzyme displayed activity towards 1-chloro-2,4-dinitrobenzene, a general GST substrate and high activities towards ethacrynic acid. It also exhibited glutathione peroxidase activity toward cumene hydroperoxide.