Gel Filtration Chromatography of Crystallins and Nucleic Acids from Different Parts of the Bovine Lens in Dependence on Age1

2015 ◽  
pp. 205-220 ◽  
Author(s):  
J. Bours ◽  
A. Wieck ◽  
O. Hockwin
Keyword(s):  
Nucleic Acids ◽  
Gel Filtration ◽  
Gel Filtration Chromatography ◽  
Bovine Lens ◽  
Different Parts

scholarly journals Determination the titer antibodies against LPS extracted from Pseudomonas aeruginosa isolated from eye infection

2012 ◽  
Vol 6 (2) ◽  
pp. 57-66
Author(s):  
Jinan M. Hasan ◽  
Rasmyia A. Abu-risha ◽  
May T. Flayyih
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Chemical Analysis ◽  
Nucleic Acids ◽  
Digestive Enzyme ◽  
Gel Filtration ◽  
Biochemical Tests ◽  
Gel Filtration Chromatography ◽  
Result Show ◽  
Eye Infection ◽  
Phenol Water

rom September 2008 to May 2009, 122 specimens were collected by sterile cotton swaps from patients suffering from eye infection at Ibn Al-Haitham Teaching Eye Hospital, 12 of them (9.83% isolation percentage) were diagnosed as Pseudomonas aeruginosa isolates by using biochemical tests, API 20 E system: they were named (P(1), P(2),……..P(12)). The agglutination sera for the grouping of P. aeruginosa test show that all the isolates belong to the P. aeruginosa strains (6, 9, 12, 16). The result show that P10 isolate have a greater ability to adhesion when all P. aeruginosa isolates were tested on Congo red agar medium and adherence to smooth surfaces. The chemical analysis of crude LPS that was extracted from P10 by using digestive enzyme and hot phenol water method showed that the percentage of carbohydrates was 7.3 and the percentage of protein was 1.3. No nucleic acids were found while the chemical analysis of partially purified LPS that was made by gel-filtration chromatography by using Sephacryl 200 S showed that the percentage of carbohydrates in the partial purified LPS was 19.5% and the percentage of binding proteins was 0.006%. No nucleic acids were found. When the molecular weight of LPS was measured by gel-filtration chromatography by using Sepharose C1- 6B- 200 it was found to be 630957 Dalton. The sera were prepared by using two wild type rabbits (weight 2-2.5 kg). They were injected with five doses over 70 days of different concentrations of partially purified LPS that have been extracted from P. aeruginosa P (10) isolate. One rabbit was used as a control that has been injected with PBS. The titer of antibodies in sera was determined by passive haemagglutination and it was in the immunized rabbit’s sera 160, and the best concentration of LPS was 10µg.

scholarly journals Analysis of serum lipoproteins by high performance gel filtration chromatography.

1996 ◽  
Vol 45 (1) ◽  
pp. 103-106 ◽  
Author(s):  
Takashi KITAMURA ◽  
Seiji ITO ◽  
Yoshio KATO ◽  
Keiko SASAMOTO ◽  
Mitsuyo OKAZAKI
Keyword(s):  
High Performance ◽  
Gel Filtration ◽  
Serum Lipoproteins ◽  
Gel Filtration Chromatography

scholarly journals Structural and Functional Conversion of Molecular Chaperone ClpB from the Gram-Positive Halophilic Lactic Acid Bacterium Tetragenococcus halophilus Mediated by ATP and Stress

2006 ◽  
Vol 188 (23) ◽  
pp. 8070-8078 ◽  
Author(s):  
Shinya Sugimoto ◽  
Hiroyuki Yoshida ◽  
Yoshimitsu Mizunoe ◽  
Keigo Tsuruno ◽  
Jiro Nakayama ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacterium ◽  
Molecular Chaperone ◽  
Thermal Inactivation ◽  
Gel Filtration ◽  
Ring Structure ◽  
Stress Conditions ◽  
Gel Filtration Chromatography ◽  
Gram Positive ◽  
Tetragenococcus Halophilus

ABSTRACT In this study, we report the purification, initial structural characterization, and functional analysis of the molecular chaperone ClpB from the gram-positive, halophilic lactic acid bacterium Tetragenococcus halophilus. A recombinant T. halophilus ClpB (ClpB Tha ) was overexpressed in Escherichia coli and purified by affinity chromatography, hydroxyapatite chromatography, and gel filtration chromatography. As demonstrated by gel filtration chromatography, chemical cross-linking with glutaraldehyde, and electron microscopy, ClpB Tha forms a homohexameric single-ring structure in the presence of ATP under nonstress conditions. However, under stress conditions, such as high-temperature (>45°C) and high-salt concentrations (>1 M KCl), it dissociated into dimers and monomers, regardless of the presence of ATP. The hexameric ClpB Tha reactivated heat-aggregated proteins dependent upon the DnaK system from T. halophilus (KJE Tha ) and ATP. Interestingly, the mixture of dimer and monomer ClpB Tha , which was formed under stress conditions, protected substrate proteins from thermal inactivation and aggregation in a manner similar to those of general molecular chaperones. From these results, we hypothesize that ClpB Tha forms dimers and monomers to function as a holding chaperone under stress conditions, whereas it forms a hexamer ring to function as a disaggregating chaperone in cooperation with KJE Tha and ATP under poststress conditions.

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