Active respiratory syncytial virus purified by ion-exchange chromatography: characterization of binding and elution requirements

1992 ◽  
Vol 38 (2) ◽  
pp. 215-228 ◽  
Author(s):  
Lou Ann Downing ◽  
Jack M. Bernstein ◽  
Anne Walter
Keyword(s):  
Respiratory Syncytial Virus ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Syncytial Virus

Proteolysis in Heterocyst-Forming Cyanobacteria: Characterization of a Further Enzyme with Trypsin-Like Specificity, and of a Prolyl Endopeptidase from Anabaena variabilis

1994 ◽  
Vol 49 (1-2) ◽  
pp. 70-78 ◽  
Author(s):  
Ulrike Strohmeier ◽  
Christian Gerdes ◽  
Wolfgang Lockau
Keyword(s):  
Ion Exchange ◽  
Proteolytic Enzymes ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Anabaena Variabilis ◽  
Prolyl Endopeptidase ◽  
Cyanobacterium Anabaena

Soluble extracts of the cyanobacterium Anabaena variabilis ATCC 29413 and an engineered mutant that lacks an intracellular protease cleaving after Lys and Arg (Maldener, Lockau, Cai, and Wolk, Mol. Gen. Genet. 225, 113-120 (1991)) were separated by ion exchange chromatography, and protease profiles determined using azocasein, Nα-benzoyl-ᴅ,ʟ arginine- 4-nitroanilide and N-carbobenzoxy-glycyl-ʟ-proline-4-nitroanilide as substrates. A second enzyme cleaving at the carboxyl side of lysine and arginine, and a prolyl endopeptidase were detected, enriched and characterized. Both proteolytic enzymes appear to be located in the periplasm.

scholarly journals Biochemical Characterization of a Thiol-Activated, Oxidation Stable Keratinase from Bacillus pumilus KS12

2010 ◽  
Vol 2010 ◽  
pp. 1-7 ◽  
Author(s):  
Rinky Rajput ◽  
Richa Sharma ◽  
Rani Gupta
Keyword(s):  
Ion Exchange ◽  
Bacillus Pumilus ◽  
Biochemical Characterization ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Amidolytic Activity ◽  
Alkaline Serine Protease ◽  
Sds Page ◽  
Temperature Optima

An extracellular keratinase from Bacillus pumilus KS12 was purified by DEAE ion exchange chromatography. It was a 45 kDa monomer as determined by SDS PAGE analysis. It was found to be an alkaline, serine protease with pH and temperature optima of 10 and 60C, respectively. It was thiol activated with two- and eight-fold enhancement in presence of 10 mM DTT and β-mercaptoethanol, respectively. In addition, its activity was stimulated in the presence of various surfactants, detergents, and oxidizing agents where a nearly 2- to 3-fold enhancement was observed in presence of H2O2 and NaHClO3. It hydrolyzed broad range of complex substrates including feather keratin, haemoglobin, fibrin, casein,and α-keratin. Analysis of amidolytic activity revealed that it efficiently cleaved phenylalanine → leucine → alanine- p-nitroanilides. It also cleaved insulin B chain between Val2- Asn3, Leu6-Cys7 and His10-Leu11 residues.

Characterization of Three 'Active' Rhodium(III) Hydroxides

1995 ◽  
Vol 48 (3) ◽  
pp. 557 ◽  
Author(s):  
SJ Crimp ◽  
L Spiccia
Keyword(s):  
Thermal Analysis ◽  
Thermal Decomposition ◽  
Infrared Spectroscopy ◽  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
X Ray Diffraction ◽  
X Ray

Pure solutions of [ Rh (H2O)6]3+, dimer [Rh2(μ-OH)2(H2O)8]4+ and trimer [Rh3(μ-OH)4(H2O)10]5+ have been converted into their respective 'active' hydroxides by dropwise addition to an imidazole solution. These 'active' hydroxides have been analysed by a variety of techniques including rhodium determination, infrared spectroscopy, thermal analysis and powder X-ray diffraction. Purity determinations using ion-exchange chromatography showed that the three hydroxides consist primarily of the neutral forms of the starting aqua ion (>96%) with small amounts of species with higher nuclearity. Rhodium analysis and thermogravimetric measurements confirmed the composition of these hydroxides to be Rh (OH)3(H2O)3.H2O, Rh2(μ-OH)2(OH)4(H2O)4 and Rh3(μ-OH)4(OH)5(H2O)5.5H2O. A scheme for the thermal decomposition of each of the hydroxides has been proposed on the basis of the t.g . and d.t.a . data and the knowledge that the final product in each case is α-Rh2O3. Heating of the hydroxides in air resulted in oxidation of RhIII to RhIV (temperature 250-300°C) forming RhO2 which on further heating decomposed to α-Rh2O3 and dioxygen.

Enolase from Lobster (Homarus americanus)

1971 ◽  
Vol 28 (6) ◽  
pp. 879-882 ◽  
Author(s):  
M. John Chapman ◽  
Christopher Chin ◽  
Finn Wold
Keyword(s):  
Heat Treatment ◽  
Ion Exchange ◽  
Ammonium Sulfate ◽  
Catalytic Properties ◽  
Gel Filtration ◽  
Homarus Americanus ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Acetone Fractionation

Enolase has been isolated from lobster muscle by acetone fractionation, heat treatment, ammonium sulfate fractionation, gel filtration, and ion-exchange chromatography. Preliminary characterization of the pure enzyme shows that the catalytic properties are very similar to those of the enolases from rabbit and fish.

scholarly journals High-Sulphur Proteins From a-Keratins ll. Isolation and Partial Characterization of Purified Components From Mouse Hair

1976 ◽  
Vol 29 (2) ◽  
pp. 11 ◽  
Author(s):  
Robert C Marshall ◽  
JM Gillespie
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Ion Exchange ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography ◽  
Fractional Precipitation ◽  
Molecular Weight Range

The present paper continues the study of the reduced and S-carboxymethylated high-sulphur proteins from mouse hair. Fractions have been obtained in a substantially purified form by fractional precipitation with ammonium sulphate at pH 6, followed by ion exchange chromatography on cellulose phosphate at pH 2�6. Approximately 80% by weight of the high-sulphur proteins fall into the ultra-high-sulphur category (carboxymethyicysteine content greater than 26 residues per 100 residues), and they cover a molecular weight range of 17000-28000. The components show a remarkable diversity in amino acid composition; for example the contents of arginine and glycine each vary by about 3 : 1. The remainder of the proteins contain 17-20 residues per 100 residues of carboxymethyicysteine, are smaller in size (molecular weight 11 500), and also show great diversity in overall amino acid composition.

Ion-exchange chromatography for the characterization of biopharmaceuticals

2015 ◽  
Vol 113 ◽  
pp. 43-55 ◽  
Author(s):  
Szabolcs Fekete ◽  
Alain Beck ◽  
Jean-Luc Veuthey ◽  
Davy Guillarme
Keyword(s):  
Ion Exchange ◽  
Ion Exchange Chromatography ◽  
Exchange Chromatography
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