scholarly journals Ammonium Sulfate Fractionation of Antibodies

2018 ◽  
Vol 2018 (6) ◽  
pp. pdb.prot099119 ◽  
Author(s):  
Jordan B. Fishman ◽  
Eric A. Berg
Keyword(s):  
Ammonium Sulfate ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

Purification and some properties of the glutamate dehydrogenase of Salmonella typhimurium

1973 ◽  
Vol 19 (4) ◽  
pp. 427-438 ◽  
Author(s):  
J. W. Coulton ◽  
M. Kapoor
Keyword(s):  
Salmonella Typhimurium ◽  
Glutamate Dehydrogenase ◽  
Ammonium Sulfate ◽  
Gradient Centrifugation ◽  
Guanidine Hydrochloride ◽  
Gel Filtration ◽  
Sedimentation Coefficient ◽  
Sucrose Density Gradient Centrifugation ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

NADP-specific glutamate dehydrogenase (GDH) from Salmonella typhimurium was purified 190-fold by heat treatment, ammonium sulfate fractionation, DEAE-Sephadex chromatography, reverse ammonium sulfate fractionation, and gel filtration. The enzyme proved to be stable to 55 °C, and displayed a pH optimum at 8.6 in the amination reaction. The sedimentation coefficient of GDH, as determined by sucrose density gradient centrifugation, was about 10.3 S. From gel filtration chromatography, the molecular weight and Stokes' radius for the enzyme were estimated at 280 000 daltons and 54 × 10−8 cm, respectively. Unusual resistance was displayed by the enzyme to high concentrations of the protein denaturants, urea, SDS, and guanidine hydrochloride.

Sensitivity of some Erwinia carotovora serogroups to macromolecular bacteriocins

1980 ◽  
Vol 26 (9) ◽  
pp. 1023-1028 ◽  
Author(s):  
C. F. Crowley ◽  
S. H. de Boer
Keyword(s):  
Electron Microscopy ◽  
Ammonium Sulfate ◽  
High Speed ◽  
Erwinia Carotovora ◽  
Bacterial Cells ◽  
Bacteriocin Activity ◽  
Specific Absorption ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

Representative strains from each of 18 Erwinia carotovora serogroups were tested for bacteriocin activity. Eight bacteriocin producing strains were found and the bacteriocins partially purified by ammonium sulfate fractionation and high-speed centrifugation. Bacteriocins from all eight strains were morphologically similar to bacteriophage tails. Specific absorption of bacteriocins from one of the antagonistic strains to sensitive bacterial cells was demonstrated with electron microscopy. In four of the serogroups tested each strain was sensitive to only one or two of the bacteriocins while in other serogroups sensitivity varied. Strains of both E. carotovora var. atroseptica and E. carotovora var. carotovora were sensitive to the same bacteriocins, but the two serogroups of var. atroseptica could be differentiated from each other on the basis of sensitivity to one bacteriocin.

scholarly journals BACTERICIDAL SUBSTANCE FROM STAPHYLOCOCCUS AUREUS

1970 ◽  
Vol 131 (5) ◽  
pp. 1004-1015 ◽  
Author(s):  
Adnan S. Dajani ◽  
Ernest D. Gray ◽  
Lewis W. Wannamaker
Keyword(s):  
Staphylococcus Aureus ◽  
Ammonium Sulfate ◽  
Phage Type ◽  
Gel Filtration ◽  
Considerable Degree ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation ◽  
Extracellular Products ◽  
Group Ii ◽  
Degree Of Purification

A bactericidal substance previously isolated from phage type 71 Slaphylococcus aureus has been further identified and characterized. Staphylococci belonging to phage type 71 produce the substance in higher titers than staphylococci lysed by other phages in group II in addition to phage 71. Other staphylococci do not produce the bactericidal substance. The bactericidal substance shares several of the properties of bacteriocins but differs from this group of antibiotic substances in some respects. A combination of ammonium sulfate fractionation and gel filtration on a Sephadex G-100 column resulted in considerable degree of purification of the bactericidal substance. The substance is a previously unrecognized product of S. aureus and is distinct from other extracellular products of this organism.

scholarly journals Antiretroviral activity of Pterois volitans (red lionfish) venom in the early development of human immunodeficiency virus/acquired immunodeficiency syndrome antiretroviral alternative source

2019 ◽  
Vol 12 (2) ◽  
pp. 309-315 ◽  
Author(s):  
Andy Noorsaman Sommeng ◽  
R. Muhammad Yusuf Arya ◽  
Mikael Januardi Ginting ◽  
Diah Kartika Pratami ◽  
Heri Hermansyah ◽  
...  
Keyword(s):  
Human Immunodeficiency Virus ◽  
Ammonium Sulfate ◽  
Phosphate Buffer ◽  
Sodium Dodecyl ◽  
Pterois Volitans ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation ◽  
Purity Analysis ◽  
Immunodeficiency Virus ◽  
Antiretroviral Activity

Aim: This study aimed to investigate the antiviral activity of Pterois volitans phospholipase A2 (PV-PLA2) from Indonesia to human immunodeficiency virus (HIV). Materials and Methods: Fresh venomous fin parts of wild PV specimens were collected from Java Sea waters. Then, it washed using phosphate buffer pH 7.0 and immersed in phosphate buffer pH 7.0 0.01 m containing CaCl2 0.001 m for 24 h. The immersed fin then allowed for extraction process by sonicating for 2×8 min with 80% pulse and 20 kHz output with temperature controlling to avoid denaturation. The crude venom (CV) extracted from the fin is allowed for purification by 80% ethanol (ET) precipitation and ammonium sulfate fractionation method. The purified PV-PLA2 then analyzed using Lowry's method, Marinette's method, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and 3-(4, 5-dimethyl thiazol-2yl)-2, 5-diphenyl tetrazolium bromide assay. After determining the purest and safest sample of six samples analyzed, the chosen sample then tested into simian retrovirus-2 (SRV2)-A549 culture (48×104 cells/mL at 1-4 ppm), and compared to the CV sample (1-4 ppm) and lamivudine (100 ppm). The culture then is analyzed using a quantitative real time-polymerase chain reaction to find out the copy number of SRV-2 virus in each culture. Results: The protein's activity, concentration, and purity analysis revealed that the PV-PLA2 purified using ammonium sulfate fractionation has the highest activity (1.81 times higher than the CV at 80% fractionation) and has higher purity than the sample from ET fractionation. The testing of the sample purified using ammonium sulfate fractionation at 80% saturation level shown that it has a 97.78% inhibition level toward SRV2-A549 culture at 4 ppm. However, in comparison to lamivudine which has 99.55% inhibition level at 100 ppm, it needs much lower concentration to achieve the same result. Conclusion: The significant inhibition of SRV2-A549 culture shown that the PV-PLA2 extracted from PV venom has the potential to become anti-HIV substances. It would be worthwhile to further evaluate the antiretroviral activity of PV-PLA2 in the in vivo studies.

scholarly journals Studying Some Properties of Amylases Extracted from `d'Anjou' Pears

HortScience ◽  
1993 ◽  
Vol 28 (4) ◽  
pp. 317-319 ◽  
Author(s):  
S.J. Li ◽  
T.J. Facteau ◽  
P. Chen
Keyword(s):  
Enzyme Activity ◽  
Ammonium Sulfate ◽  
Specific Activity ◽  
Pyrus Communis ◽  
Assay System ◽  
Acetate Buffer ◽  
Starch Degradation ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

Several characteristics of amylases involved in starch degradation were studied in extracts from immature (30 days before harvest) `d'Anjou' pears (Pyrus communis L.). Enzyme activity was not detected until after at least 60 minutes of incubation in frozen or lyophilized tissues. Activity increased significantly after 90 minutes and increased linearly after 2 to 12 hours of incubation. Activity was greater, however, in frozen than in lyophilized tissues. Three buffers (acetate, tris-HCl, and imidazole-HCl) were used at a range of pH levels (4.6-8.2) to ascertain the optimum assay system. Highest specific activity was recorded with acetate buffer at pH 5.6. The Km value in this system was 1.43 × 10-3g·ml-1. Specific activity increased as Ca concentration in the reaction mixture increased from 1 to 15 mm CaCl2 but did not change as Ca concentration increased from 15 to 25 mm CaCl2. The `d'Anjou' pear amylases were purified 5.7-fold using ammonium sulfate fractionation.

Purification and characterization of a lytic peptidase produced by Bdellovibrio bacteriovorus 6-5-S

1973 ◽  
Vol 19 (5) ◽  
pp. 659-666 ◽  
Author(s):  
H. B. Fackrell ◽  
J. Robinson
Keyword(s):  
Molecular Weight ◽  
Ammonium Sulfate ◽  
Gel Filtration ◽  
Culture Fluid ◽  
Diaminopimelic Acid ◽  
Lytic Enzyme ◽  
Bdellovibrio Bacteriovorus ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

Bdellovibrio bacteriovorus 6-5-S releases at least two enzymes into the culture fluid when grown on autoclaved cells of Spirillum serpens VHL. One of the enzymes is bacteriolytic and the other is proteolytic. The lytic enzyme was purified by a factor of 3000 using ammonium sulfate fractionation, Sephadex G-100 gel filtration, and the anion exchanger DEAE-Sephadex. The lytic enzyme degrades peptidoglycan of S. serpens by hydrolyzing the diaminopimelic acid – alanine bond in the tetrapeptide chain. Ca2+ or Mg2+ exerted little or no effect on the activity of the lytic enzyme. The enzyme had a molecular weight of 40 000 as indicated by gel filtration. Crude preparations were unstable at 4C. The second enzyme, a protease that digested Azocoll, was purified by a factor of 7 by ammonium sulfate fractionation followed by gel filtration with Sephadex G-100. The protease was eluted in the void volume from a Sephadex G-100 column and therefore may have a molecular weight of at least 100 000. Its activity was enhanced by additions of Ca2+ and Mg2+. The enzyme was stable at 4C.

Purification of a Fibrinolytic Protein from the Yellow Mealworm Beetles, Tenebrio Molitor

2011 ◽  
Vol 396-398 ◽  
pp. 103-105
Author(s):  
Lei Yu ◽  
Ya Li Han ◽  
Zhu Jun Tan
Keyword(s):  
Molecular Mass ◽  
Ammonium Sulfate ◽  
Fibrinolytic Activity ◽  
Tenebrio Molitor ◽  
Relative Molecular Mass ◽  
Yellow Mealworm ◽  
Chromatography Column ◽  
Ammonium Sulfate Fractionation ◽  
Sulfate Fractionation

A novel of fibrinolytic protein was isolated from the Tenebrio molitor, using three purification steps (ammonium sulfate fractionation, DEAE-32 cellulose chromatography column, and SephadexG-75 dextran gel column). After testing, the protein from Tenebrio molitor has fibrinolytic activity, and it relative molecular mass was 56.1 kD.

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