HPLC Measurement of the Uronate and Neutral Sugar Contents in Corn Hemicellulose

1993 ◽  
Vol 57 (7) ◽  
pp. 1191-1192 ◽  
Author(s):  
Fumihide Yamaguchi ◽  
Chitoshi Hatanaka
Keyword(s):  
Neutral Sugar ◽  
Hplc Measurement

Biodecomposition of Phenanthrene and Pyrene by a Genetically Engineered Escherichia coli

2020 ◽  
Vol 14 (2) ◽  
pp. 121-133 ◽  
Author(s):  
Maryam Ahankoub ◽  
Gashtasb Mardani ◽  
Payam Ghasemi-Dehkordi ◽  
Ameneh Mehri-Ghahfarrokhi ◽  
Abbas Doosti ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
High Performance ◽  
Human Cancer ◽  
Genetically Engineered ◽  
Hazardous Substances ◽  
E Coli ◽  
Spiked Soil ◽  
Engineered Escherichia Coli ◽  
Genetically Manipulated ◽  
Hplc Measurement

Background: Genetically engineered microorganisms (GEMs) can be used for bioremediation of the biological pollutants into nonhazardous or less-hazardous substances, at lower cost. Polycyclic aromatic hydrocarbons (PAHs) are one of these contaminants that associated with a risk of human cancer development. Genetically engineered E. coli that encoded catechol 2,3- dioxygenase (C230) was created and investigated its ability to biodecomposition of phenanthrene and pyrene in spiked soil using high-performance liquid chromatography (HPLC) measurement. We revised patents documents relating to the use of GEMs for bioremediation. This approach have already been done in others studies although using other genes codifying for same catechol degradation approach. Objective: In this study, we investigated biodecomposition of phenanthrene and pyrene by a genetically engineered Escherichia coli. Methods: Briefly, following the cloning of C230 gene (nahH) into pUC18 vector and transformation into E. coli Top10F, the complementary tests, including catalase, oxidase and PCR were used as on isolated bacteria from spiked soil. Results: The results of HPLC measurement showed that in spiked soil containing engineered E. coli, biodegradation of phenanthrene and pyrene comparing to autoclaved soil that inoculated by wild type of E. coli and normal soil group with natural microbial flora, were statistically significant (p<0.05). Moreover, catalase test was positive while the oxidase tests were negative. Conclusion: These findings indicated that genetically manipulated E. coli can provide an effective clean-up process on PAH compounds and it is useful for bioremediation of environmental pollution with petrochemical products.

Strain distribution and in planta production of an extracellular polysaccharide depolymerase from Bradyrhizobium japonicum

1992 ◽  
Vol 38 (8) ◽  
pp. 857-861 ◽  
Author(s):  
Michael F. Dunn ◽  
Arthur L. Karr
Keyword(s):  
Bradyrhizobium Japonicum ◽  
Root Nodules ◽  
Extracellular Polysaccharide ◽  
Extracellular Polysaccharides ◽  
Neutral Sugar ◽  
In Planta ◽  
In Vitro Production ◽  
Polysaccharide Composition ◽  
Vitro Production

Thirty-four strains of Bradyrhizobium japonicum were screened for the in vitro production of an extracellular polysaccharide depolymerase active against the B. japonicum acidic extracellular polysaccharide that contains mannose, glucose, galactose, and 4-O-methylgalactose as neutral sugar components. Over 90% of tested strains producing this type of extracellular polysaccharide also produced the extracellular polysaccharide depolymerase, whereas strains producing a compositionally different extracellular polysaccharide did not. In addition, representatives of species related to B. japonicum by extracellular polysaccharide composition or host range were also phenotypically depolymerase negative. Depolymerase was also present in soybean root nodules formed by B. japonicum strain 2143. In contrast to the cell-associated depolymerase activity found in free-living cells of this strain, most of the depolymerase activity present in nodules is free of the bacteroids. The widespread occurrence of the depolymerase among B. japonicum strains and the spatiotemporal distribution of its activity in planta are consistent with the enzyme playing a role in the removal of surface extracellular polysaccharide from the microorganism during the infection of nodulation process. Key words: Bradyrhizobium japonicum, soybean, extracellular polysaccharides, extracellular polysaccharide depolymerase, bacteroids.

scholarly journals Resolution, purification and some properties of the multiple forms of cellobiose quinone dehydrogenase from the white-rot fungus Sporotrichum pulverulentum

1986 ◽  
Vol 236 (1) ◽  
pp. 221-226 ◽  
Author(s):  
F F Morpeth ◽  
G D Jones
Keyword(s):  
Superoxide Anion ◽  
Sugar Content ◽  
White Rot ◽  
Sedimentation Equilibrium ◽  
White Rot Fungus ◽  
Neutral Sugar ◽  
Apparent Difference ◽  
Multiple Forms ◽  
Sporotrichum Pulverulentum ◽  
Similar Kinetic

Four forms of cellobiose quinone dehydrogenase have been purified from the white-rot fungus Sporotrichum pulverulentum. The Mr of the enzyme has been estimated by sedimentation equilibrium to be 57,800 and by SDS/polyacrylamide-gel to be 60,000. These enzymes are clearly monomers. Cellobiose quinone dehydrogenases contain FAD and variable amounts of a green chromophore which we suggest is 6-hydroxy-FAD. The superoxide anion and H2O2 are the products of its reaction with oxygen. All of the isoenzymes from any one preparation display similar kinetic parameters. However, these vary between preparations. The only apparent difference between the four separable isoenzymes is their neutral-sugar content.

Interference of hemoglobin (Hb) Las Palmas with HPLC measurement of HbA1c in 87 patients

2012 ◽  
Vol 50 (2) ◽  
Author(s):  
Mercedes Lorenzo-Medina ◽  
Silvia De La Iglesia ◽  
Paloma Ropero ◽  
Mercedes Navarro-Romero ◽  
Ruth Martín-Alfaro ◽  
...  
Keyword(s):  
Hplc Measurement

scholarly journals Role of maltase in the utilization of sucrose by Candida albicans

1993 ◽  
Vol 291 (3) ◽  
pp. 765-771 ◽  
Author(s):  
P R Williamson ◽  
M A Huber ◽  
J E Bennett
Keyword(s):  
Candida Albicans ◽  
Intracellular Localization ◽  
Cross Reactivity ◽  
Neutral Sugar ◽  
Sequence Specificity ◽  
Western Blots ◽  
Sds Page ◽  
Molecular Masses ◽  
Kinetics Of

Two isoenzymes of maltase (EC 3.2.1.20) were purified to homogeneity from Candida albicans. Isoenzymes I and II were found to have apparent molecular masses of 63 and 66 kDa on SDS/PAGE with isoelectric points of 5.0 and 4.6 respectively. Both isoenzymes resembled each other in similar N-terminal sequence, specificity for the alpha(1-−>4) glycosidic linkage and immune cross-reactivity on Western blots using a maltase II antigen-purified rabbit antibody. Maltase was induced by growth on sucrose whereas beta-fructofuranosidase activity could not be detected under similar conditions. Maltase I and II were shown to be unglycosylated enzymes by neutral sugar assay, and more than 90% of alpha-glucosidase activity was recoverable from spheroplasts. These data, in combination with other results from this laboratory [Geber, Williamson, Rex, Sweeney and Bennett (1992) J. Bacteriol. 174, 6992-6996] showing lack of a plausible leader sequence in genomic or mRNA transcripts, suggest an intracellular localization of the enzyme. To establish further the mechanism of sucrose assimilation by maltase, the existence of a sucrose-inducible H+/sucrose syn-transporter was demonstrated by (1) the kinetics of sucrose-induced [14C]sucrose uptake, (2) recovery of intact [14C]sucrose from ground cells by t.l.c. and (3) transport of 0.83 mol of H+/mol of [14C]sucrose. In total, the above is consistent with a mechanism whereby sucrose is transported into C. albicans to be hydrolysed by an intracellular maltase.

scholarly journals Lipophilic O-antigens containing D-glycero-D-mannoheptose as the sole neutral sugar in Rhodopseudomonas gelatinosa.

1975 ◽  
Vol 123 (2) ◽  
pp. 449-455 ◽  
Author(s):  
J Weckesser ◽  
H Mayer ◽  
G Drews ◽  
I Fromme
Keyword(s):  
Neutral Sugar ◽  
O Antigens

Differences in the biochemical compositions and elicitor activity of extracellular components produced by three races of a fungal plant pathogen, Colletotrichum lindemuthianum

1980 ◽  
Vol 26 (12) ◽  
pp. 1473-1479 ◽  
Author(s):  
Aaanne J. Anderson
Keyword(s):  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Colletotrichum Lindemuthianum ◽  
Neutral Sugar ◽  
Sugar Composition ◽  
Fungal Plant Pathogen ◽  
Red Kidney Bean ◽  
Weakly Virulent ◽  
Protein Components ◽  
Highly Virulent

High molecular weight products from the α, β, and γ races of Colletotrichum lin-differed in their carbohydrate and protein compositions and in their abilities to elicit symptoms of a hypersensitive response in dark red kidney bean. The neutral sugar composition of the products varied in their proportions of rhamnose, mannose, galactose, and glucose. Polyacrylamide gel electrophoresis showed the protein components to be more numerous in the β race products than in the α or γ race products. Each protein band co-stained for carbohydrate. Highest elicitor activity was observed in the products from the α race, a race avirulent on dark red kidney. The products from the weakly virulent γ race were about 10-fold less active as elicitors than those of the α race. With the β race, a race highly virulent on dark red kidney, elicitor activity was 100-fold less than that of the α race.

Purification and characterization of a Ca2+-dependent novel lectin from Nymphaea nouchali tuber with antiproliferative activities

2011 ◽  
Vol 31 (6) ◽  
pp. 465-475 ◽  
Author(s):  
Syed Rashel Kabir ◽  
Md. Abu Zubair ◽  
Md. Nurujjaman ◽  
Md. Azizul Haque ◽  
Imtiaj Hasan ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Pathogenic Bacteria ◽  
Sequence Similarity ◽  
Deae Cellulose ◽  
Ehrlich Ascites Carcinoma ◽  
Anion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Neutral Sugar ◽  
The Stability

A lectin (termed NNTL) was purified from the extracts of Nymphaea nouchali tuber followed by anion-exchange chromatography on DEAE-cellulose, hydrophobic chromatography on HiTrap Phenyl HP and by repeated anion-exchange chromatography on HiTrap Q FF column. The molecular mass of the purified lectin was 27.0 ± 1.0 kDa, as estimated by SDS/PAGE both in the presence and in the absence of 2-mercaptoethanol. NNTL was an o-nitrophenyl β-D-galactopyranoside sugar-specific lectin that agglutinated rat, chicken and different groups of human blood cells and exhibited high agglutination activity over the pH range 5–9 and temperatures of 30–60°C. The N-terminal sequence of NNTL did not show sequence similarity with any other lectin and the amino acid analysis revealed that NNTL was rich in leucine, methionine and glycine residues. NNTL was a glycoprotein containing 8% neutral sugar and showed toxicity against brine shrimp nauplii with an LC50 value of 120 ± 29 μg/ml and exerted strong agglutination activity against four pathogenic bacteria (Bacillus subtilis, Sarcina lutea, Shigella shiga and Shigella sonnei). In addition, antiproliferative activity of this lectin against EAC (Ehrlich ascites carcinoma) cells showed 56% and 76% inhibition in vivo in mice at 1.5 and 3 mg·kg−1·day−1 respectively. NNTL was a divalent ion-dependent glycoprotein, which lost its activity markedly in the presence of denaturants. Furthermore, measurement of fluorescence spectra in the presence and absence of urea and CaCl2 indicated the requirement of Ca2+ for the stability of NNTL.

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