• Title/Summary/Keyword: G Proteins

Search Result 1,766, Processing Time 0.025 seconds

Proteomic Studies in Plants

  • Park, Ohk-Mae K.
    • BMB Reports
    • /
    • v.37 no.1
    • /
    • pp.133-138
    • /
    • 2004
  • Proteomics is a leading technology for the high-throughput analysis of proteins on a genome-wide scale. With the completion of genome sequencing projects and the development of analytical methods for protein characterization, proteomics has become a major field of functional genomics. The initial objective of proteomics was the large-scale identification of all protein species in a cell or tissue. The applications are currently being extended to analyze various functional aspects of proteins such as post-translational modifications, protein-protein interactions, activities and structures. Whereas the proteomics research is quite advanced in animals and yeast as well as Escherichia coli, plant proteomics is only at the initial phase. Major studies of plant proteomics have been reported on subcellular proteomes and protein complexes (e.g. proteins in the plasma membranes, chloroplasts, mitochondria and nuclei). Here several plant proteomics studies will be presented, followed by a recent work using multidimensional protein identification technology (MudPIT).

Polyacrylamide Gel Electrophoresis on Ginseng Proteins (인삼 단백질분획에 대한 폴리아크릴아미드 전기영동)

  • 김춘미;황정주
    • YAKHAK HOEJI
    • /
    • v.30 no.6
    • /
    • pp.343-347
    • /
    • 1986
  • Korean ginseng was purified to obtain radioprotective protein fractions by buffer extraction, ammonium sulfate fractionation, CM-cellulose column chromatography, heat inactivation and Sephadex G-75 column chromatography. The final three fractions, GI, GII and GIII were subjected to Disc-polyacrylamide gel electrophoresis (PAGE) and SDS-PAGE. The molecular weights(M.W.) of native and denatured proteins were estimated by using regression line equations obtained from the mobilities of standard proteins. As the results, in Disc-PAGE, the GI fraction showed two protein bands with M.W. of above 213, 000 and 55, 000, GII showed one band with M.W. of 44, 000 and GIII, also one band with M.W. of 19, 000. In SDS-PAGE, GI fraction gave four subunit bands with M.W. of above 114, 000, 27, 000, 24, 000 and 19, 000, GII gave two bands with M.W. of 46, 000 and 22, 000, and GIII, one band of 19, 000.

  • PDF

Active role of oxygen on penicillin sensitivity and fromation of membrane protein in escherichia coli K12 (Escherichia coli K12의 막단백질 형성과 페니실린 민감성에 대한 산소의 능동적 역할)

  • 박현근;한홍의
    • Korean Journal of Microbiology
    • /
    • v.24 no.3
    • /
    • pp.263-269
    • /
    • 1986
  • Membrane proteins of facultatively anaerobic Escherichia coli K12 which was logarithmically grown in aerobiosis and anaerobiosis were compared on 5 to 10% liner gradient gel electrophoresis (Na Dod $SO_4 -PAGE$). Membrane proteins were formed as different patterns between aerobiosis and anaerobiosis. Among them, 91Kdal protein (pbp1a) was not synthesized in aerobiosis and 60Kdal protein (fts cluster), in anaerobiosis. Thereby cells cultured aerobically were differenciated as diversiform cell shape, comparing cells cultured anaerobically and the latter were resistant to penicillin G. Thus it is believed that in facultative anaerobes atmospheric oxygen regulated the synthesis of membrane proteins and even the expression of equivalent genes, and moreover alleviated the resistance to an antibiotic penicillin.

  • PDF

SDS-polyacrylamide Gel Electrophoresis on Partially Purified Ginseng Proteins (인삼단백질분획에 대한 SDS-폴리 아크릴아미드 전기영동)

  • 김춘미
    • YAKHAK HOEJI
    • /
    • v.27 no.4
    • /
    • pp.315-320
    • /
    • 1983
  • Ginseng proteins have been extracted and partially purified by the methods of ammonium sulfate fractionation, heat inactivation and Sephadex G-75 column chromatography. The final three fractions obtained (GI, GII and GIII) were subjected to paper chromatography and SDS-polyacrylamide gel electrophoresis. Molecular weights of polypeptide chains from each fraction were est-mated by the standard line obtained from the plot of electrophoretic mobilities against the logarithm of molecular weights of standard proteins. Results are as follows: 1) GI showed three protein spots and four polypeptides of which M.W. were 63,000, 60,000, 56,000, 51,000 and 34,200. 2) GII showed four protein spots and five polypeptides with their M.W. of 64,600, 56,000, 45,400, 35,800, end 25,200, 3) GIII showed three protein spots and four polypeptides with their M.W. of 66,000, 63,000, 56,000 and 22,000.

  • PDF

An Integrated Process for the Separation and Purification of Biologically Active Proteins from Human Urine (인뇨로부터 유용단백질의 통합 분리정제 공정)

  • 김기용;정광회문흥모
    • KSBB Journal
    • /
    • v.8 no.3
    • /
    • pp.287-294
    • /
    • 1993
  • For the purpose of combining the purification processes for several biologically active proteins form human urine, an efficient integrated fractionation procedure has been investigated. The procedure was started by concentration with ultrafiltration and pH precipitation followed by a selectable combination of chromatography on gel filtration, adsorption, ion exchanger, affinity, and reverse phase column. By this process, the purified urokinase, epidermal growth factor and albumin migrated as a single band on SDS-polyacrylamide gel electrophoresis and were fully active. The recoveries of these purified proteins were 48%, 17%, and 46%, respectively.

  • PDF

Further Purification of Radioprotective Ginseng Protein Fraction by Gel Filtration (Gel filtration에 의한 한방사선 인삼단백 분획의 정제)

  • 김춘미;박경애
    • Journal of Ginseng Research
    • /
    • v.13 no.2
    • /
    • pp.254-259
    • /
    • 1989
  • A radioprotective ginseng protein fraction was obtained from Korean white ginseng powder by the following isolation and purification procedures: Tris-HCI buffer extraction, 70% ammonium sulfate fractionation, CM-rellulosr column chromatography, heat inactivation and Sephadex G-75 column chromatography. This fraction was further purified by Sepharose 4B and Sephadex G-150 column chromatographies. Three fractions obtained were subjected to Native-PAGE and SDS-PAGE using gradient gels and the silver staining method. Molecular weights of the native proteins and their subunits were estimated.

  • PDF

Quantitative Changes of PR Proteins and Antioxidative Enzymes in Response to Glomus intraradices and Phytophthora capsici in Pepper (Capsicum annuum L.) Plants

  • Zheng, Hu-Zhe;Kim, Yong-Woong;Lee, Hyun-Jin;Park, Ro-Dong;Jung, Woo-Jin;Kim, Young-Cheol;Lee, Sang-Hyun;Kim, Tae-Hwan;Kim, Kil-Yong
    • Journal of Microbiology and Biotechnology
    • /
    • v.14 no.3
    • /
    • pp.553-562
    • /
    • 2004
  • To investigate protective activity in pepper plants, which were pre-inoculated with arbuscular mycorrhizal (AM) fungi Glomus intra radices (Gi), against pathogenic strain Phytophthora capsici (Pc), pathogenesis-related (PR) proteins and antioxidant enzymes were examined. The growth of root and shoot was the highest in peppers inoculated with G. intraradices, compared with non-inoculated control plants and those challenged by the pathogen with and without mycorrhizae after nine days of infection. Mycorrhizal colonization rate was reduced by about 10% in pathogen-challenged plants, but disease pressure was reduced. The activities of PR proteins, $\beta$-1- 3-glucanase and chitinase, were increased in Pc-treated plants compared to Gi+Pc-treated plants in leaves, but those in roots were suppressed. Superoxide dismutase activity and $H_2O_2${/TEX> content in Gi+Pc and Pc-treated plants were gradually increased in leaves. However, those in roots continuously increased up to 5 days, and then decreased dramatically. Peroxidase activity in leaves and roots increased after P. capsici infection both in plants inoculated with or without G. intraradices. These results suggest that AM fungi, G. intra radices, potentially act as one of the protective agents against plant pathogens. Changes of PR proteins and antioxidative enzymes in mycorrhizae-inoculated pepper appear to be regulated differently in leaves and roots by pathogen infection.

The Optimization of Expression System for Recombinant Protein Production by Pichia pastoris and Hansenula polymorphs (유전자 재조합 단백질 생산에 있어서 Pichia pastoris와 Hansenula polymorpha를 이용한 최적 발현 방법 개발)

  • 강환구;전희진;김재호
    • KSBB Journal
    • /
    • v.15 no.2
    • /
    • pp.174-180
    • /
    • 2000
  • Pichia pastoris and Hansenula polymorpha, the methylotrophic yeasts have been widely used as a host for the production of e eudaryotic proteins due to the advantages related to their inherited characters. This paper describes the method to enhance t the productivity of recombinant proteins by P. pastoris and H. po$\psi$morpha. In the production of recombinant proteins using a f fed batch fermentation system, the effects of specific growth rate on the specific expression rate of re$\infty$mbinant proteins w were studied. In both species, the expression system of recombinant proteins using the fed batch fermentation was optimezed.

  • PDF

Immune Response of Bacterial Proteins of Staphylococcus intermedius from Canine Atopic Dermatitis (개의 아토피성 피부염에서 분리한 Staphylococcus intermedius 균의 세균단백질의 면역반응)

  • Park, Hee-myung
    • Journal of Veterinary Clinics
    • /
    • v.21 no.1
    • /
    • pp.20-22
    • /
    • 2004
  • Bacterial infection of canine atopic dermatitis is largely caused by Staphylococcus intermedius and may be a superficial or deep pyoderma. The Purpose of this study was to identify the major proteins of S. intermedius cell surface components in humoral immune response of atopic dermatitis dog. Sera samples were obtained from dogs with atopic dermatitis and superficial pyoderma referred to the Veterinary Medical Teaching Hospital, Konkuk University. An isolate of S. intermedius from a clinical case of canine atopic dermatitis was cultured in brain heart infusion broth overnight at $37^{\circ}C$ in aerobic conditions on an orbital shaker. Following culture, Staphylococci were harvested by centrifugation, washed in PBS, and resuspended in PBS containing lysostaphin. The soluble components were separated by centrifugation and were collected. The soluble extract of S. intermedius was separated by sodium dodecylsulphate polyacrylamide gel electrophoresis (SDS-PAGE). The proteins were electrophoretically transferred onto nitrocellulose membrane. Western blotting for the specificity of serum IgG antistaphylococcal antibody was performed with anti-dog-IgG and sera obtained from an atopic dermatitis case and a normal dog. The molecular masses of four major proteins of S. intermedius recognized by serum obtained from an atopic dermatitis case were 18, 31, 75, and 110 kDa as determined by Western blot analysis. The present study indicates that most dogs of S. intermedius infection with atopic dermatitis could have a significant humoral immune response to bacterial proteins of the causative organism.

Identification of proteins involved in the pancreatic exocrine by exogenous ghrelin administration in Sprague-Dawley rats

  • Lee, Kyung-Hoon;Wang, Tao;Jin, Yong-Cheng;Lee, Sang-Bum;Oh, Jin-Ju;Hwang, Jin-Hee;Lim, Ji-Na;Lee, Jae-Sung;Lee, Hong-Gu
    • Journal of Animal Science and Technology
    • /
    • v.56 no.2
    • /
    • pp.6.1-6.4
    • /
    • 2014
  • The aims of study were to investigate the effects of intraperitoneal (i.p.) infusion of ghrelin on pancreatic ${\alpha}$-amylase outputs and the responses of pancreatic proteins to ghrelin that may relate to the pancreatic exocrine. Six male Sprague-Dawley rats (300 g) were randomly divided into two groups, a control group (C, n = 3) and a treatment group (T, $10.0{\mu}g/kg$ BW, n = 3). Blood samples were collected from rat caudal vein once time after one hour injection. The concentrations of plasma ghrelin, cholecystokinin (CCK) and alfa-amylase activity were evaluated by enzyme immunoassay (EIA) kit. Two-dimensional gel electrophoresis (2-DE) analysis was conducted to separate the proteins in pancreas tissue. Results showed that the i.p. infusion of ghrelin at doses of $10.0{\mu}g/kg$ body weight (BW) increased the plasma ghrelin concentrations (p = 0.07) and elevated the plasma CCK level significantly (p < 0.05). Although there was no statistically significant, the ${\alpha}$-amylase activity tended to increase. The proteomics analysis indicated that some pancreatic proteins with various functions were up- or down-regulated compared with control group. In conclusion, ghrelin may have role in the pancreatic exocrine, but the signaling pathway was still not clear. Therefore, much more functional studies focus on these found proteins are needed in the near future.