Two-state irreversible thermal denaturation of Euphorbia characias latex amine oxidase

2007 ◽  
Vol 125 (2-3) ◽  
pp. 254-259 ◽  
Author(s):  
Mojtaba Amani ◽  
Ali A. Moosavi-Movahedi ◽  
Giovanni Floris ◽  
Anna Mura ◽  
Boris I. Kurganov ◽  
...  
Keyword(s):  
Thermal Denaturation ◽  
Amine Oxidase ◽  
Euphorbia Characias

Euphorbia characias Latex Amine Oxidase and Peroxidase: Interacting Enzymes?

2013 ◽  
Vol 32 (6) ◽  
pp. 435-441 ◽  
Author(s):  
Francesca Pintus ◽  
Delia Spanò ◽  
Giovanni Floris ◽  
Rosaria Medda
Keyword(s):  
Amine Oxidase ◽  
Euphorbia Characias

scholarly journals Bioseparation of Four Proteins fromEuphorbia characiasLatex: Amine Oxidase, Peroxidase, Nucleotide Pyrophosphatase/Phosphodiesterase, and Purple Acid Phosphatase

2011 ◽  
Vol 2011 ◽  
pp. 1-7 ◽  
Author(s):  
Rosaria Medda ◽  
Francesca Pintus ◽  
Delia Spanò ◽  
Giovanni Floris
Keyword(s):  
Acid Phosphatase ◽  
Amine Oxidase ◽  
Deae Cellulose ◽  
Purple Acid Phosphatase ◽  
Copper Amine Oxidase ◽  
Nucleotide Pyrophosphatase ◽  
Euphorbia Characias ◽  
High Purification ◽  
Purification Methods ◽  
Different Sources

This paper deals with the purification of four proteins fromEuphorbia characiaslatex, a copper amine oxidase, a nucleotide pyrophosphatase/phosphodiesterase, a peroxidase, and a purple acid phosphatase. These proteins, very different in molecular weight, in primary structure, and in the catalyzed reaction, are purified using identical preliminary steps of purification and by chromatographic methods. In particular, the DEAE-cellulose chromatography is used as a useful purification step for all the four enzymes. The purification methods here reported allow to obtain a high purification of all the four proteins with a good yield. This paper will give some thorough suggestions for researchers busy in separation of macromolecules from different sources.

Amine oxidase from Euphorbia characias : Kinetic and structural characterization

2017 ◽  
Vol 65 (1) ◽  
pp. 81-88 ◽  
Author(s):  
Francesca Pintus ◽  
Annalaura Sabatucci ◽  
Mauro Maccarrone ◽  
Enrico Dainese ◽  
Rosaria Medda
Keyword(s):  
Structural Characterization ◽  
Amine Oxidase ◽  
Euphorbia Characias

Tyramine oxidation by copper/TPQ amine oxidase and peroxidase from Euphorbia characias latex

2008 ◽  
Vol 475 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Anna Mura ◽  
Francesca Pintus ◽  
Antonella Fais ◽  
Simona Porcu ◽  
Marcella Corda ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Euphorbia Characias

Osmolytic Effect of Sucrose on Thermal Denaturation of Pea Seedling Copper Amine Oxidase

2017 ◽  
Vol 36 (2) ◽  
pp. 147-153 ◽  
Author(s):  
Mojtaba Amani ◽  
Aboozar Barzegar ◽  
Mohammad Mazani
Keyword(s):  
Thermal Denaturation ◽  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Pea Seedling ◽  
Copper Amine

scholarly journals Characterization of Euphorbia characias Latex Amine Oxidase

1998 ◽  
Vol 117 (4) ◽  
pp. 1363-1371 ◽  
Author(s):  
Alessandra Padiglia ◽  
Rosaria Medda ◽  
Anita Lorrai ◽  
Barbara Murgia ◽  
Jens Z. Pedersen ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Euphorbia Characias

Mitochondrial Oxidation of p-N, N-Dimethylamino-β-Phenethylamine (DAPA)

1975 ◽  
Vol 33 ◽  
pp. 458-459
Author(s):  
W. Allen Shannon ◽  
Hannah L. Wasserkrug ◽  
andArnold M. Seligman
Keyword(s):  
Guinea Pig ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Histochemical Demonstration ◽  
Guinea Pig Heart ◽  
Pig Kidney ◽  
Cytoplasmic Vacuoles ◽  
Liver And Kidney ◽  
Mitochondrial Oxidation ◽  
Amine Oxidase Activity

The synthesis of a new substrate, p-N,N-dimethylamino-β-phenethylamine (DAPA)3 (Fig. 1) (1,2), and the testing of it as a possible substrate for tissue amine oxidase activity have resulted in the ultracytochemical localization of enzyme oxidase activity referred to as DAPA oxidase (DAPAO). DAPA was designed with the goal of providing an amine that would yield on oxidation a stronger reducing aldehyde than does tryptamine in the histochemical demonstration of monoamine oxidase (MAO) with tetrazolium salts.Ultracytochemical preparations of guinea pig heart, liver and kidney and rat heart and liver were studied. Guinea pig kidney, known to exhibit high levels of MAO, appeared the most reactive of the tissues studied. DAPAO reaction product appears primarily in mitochondrial outer compartments and cristae (Figs. 2-4). Reaction product is also localized in endoplasmic reticulum, cytoplasmic vacuoles and nuclear envelopes (Figs. 2 and 3) and in the sarcoplasmic reticulum of heart.

Effect of Calcium ion on the interaction between Thrombin and Heparin. Thermal Denaturation

1977 ◽  
Vol 38 (03) ◽  
pp. 0677-0684 ◽  
Author(s):  
Raymund Machovich ◽  
Péter Arányi
Keyword(s):  
Calcium Ions ◽  
Rate Constants ◽  
Thermal Denaturation ◽  
Time Course ◽  
Complex Analysis ◽  
Heat Inactivation ◽  
Second Phase ◽  
Denaturation Kinetics ◽  
Enzyme Protection ◽  
Enzyme Denaturation

SummaryHeat inactivation of thrombin at 54° C followed first order kinetics with a rate constant of 1.0 min−1 approximately. Addition of heparin resulted in protection against thermal denaturation and, at the same time, rendered denaturation kinetics more complex. Analysis of the biphasic curve of heat inactivation in the presence of heparin revealed that the rate constants of the second phase changed systematically with heparin concentrations. Namely, at 4.5 × 10−6M, 9 × 10−6M, 1.8 × 10−5M and 3.6 × 10−5M heparin concentrations, the rate constants were 0.27 min−1, 0.17 min−1, 0.11 min−1 and 0.06 min−1, respectively.Sulfate as well as phosphate ions displayed also enzyme protection against heat inactivation, however, the same effect was obtained already at a heparin concentration, lower by three orders of magnitude.The kinetics of enzyme denaturation was not affected by calcium ions, whereas in the presence of heparin the inactivation rate of thrombin changed, i. e. calcium ions abolished the biphasic character of time course of thermal denaturation.Thus, the data suggest that calcium ions contribute to the effect of heparin on thrombin.

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