IRREVERSIBLE AFFINITY IMMOBILIZATION OF LENTIL SEEDLING AMINE OXIDASE WITH ACTIVITY RETENTION

2007 ◽  
Vol 6 (1) ◽  
pp. 31-35 ◽  
Author(s):  
Enrico Sanjust ◽  
Francesca Sollai ◽  
Barbara Noli ◽  
Giovanni Floris
Keyword(s):  
Amine Oxidase ◽  
Affinity Immobilization ◽  
Lentil Seedling

scholarly journals Cysteamine oxidation by lentil seedling amine oxidase

IUBMB Life ◽  
1997 ◽  
Vol 41 (2) ◽  
pp. 395-405
Author(s):  
Rosaria Medda ◽  
Alessandra Padiglia ◽  
Anita Lorrai ◽  
Giovanni Floris ◽  
Carlo De Marco
Keyword(s):  
Amine Oxidase ◽  
Lentil Seedling

scholarly journals Thermal Dissection of Lentil Seedling Amine Oxidase Domains by Differential Scanning Calorimetry

2007 ◽  
Vol 71 (7) ◽  
pp. 1644-1649 ◽  
Author(s):  
Ali Akbar MOOSAVI-MOVAHEDI ◽  
Mojtaba AMANI ◽  
Seyedeh Zahra MOOSAVI-NEJAD ◽  
Sedigheh HASHEMNIA ◽  
Faizan AHMAD ◽  
...  
Keyword(s):  
Differential Scanning Calorimetry ◽  
Amine Oxidase ◽  
Scanning Calorimetry ◽  
Lentil Seedling

Oxidation of benzylamine Br-derivatives by lentil seedling copper-amine oxidase

2000 ◽  
Vol 134 (1) ◽  
pp. 11-18
Author(s):  
Rosaria Medda ◽  
Alessandra Padiglia ◽  
Anita Lorrai ◽  
Barbara Murgia ◽  
Giovanni Floris
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Lentil Seedling ◽  
Copper Amine

scholarly journals Conformational Lock and Dissociative Thermal Inactivation of Lentil Seedling Amine Oxidase

BMB Reports ◽  
2003 ◽  
Vol 36 (2) ◽  
pp. 167-172 ◽  
Author(s):  
S. Zahra Moosavi-Nejad ◽  
Ali-Akbar Moosavi-Movahedi ◽  
Mostafa Rezaei-Tavirani ◽  
Giovanni Floris ◽  
Rosaria Medda
Keyword(s):  
Thermal Inactivation ◽  
Amine Oxidase ◽  
Lentil Seedling

scholarly journals Substrate specificity of lentil seedling amine oxidase

IUBMB Life ◽  
1996 ◽  
Vol 40 (3) ◽  
pp. 629-637
Author(s):  
Rosaria Medda ◽  
Alessandra Padiglia ◽  
Jens Pedersen ◽  
Anita Lorrai ◽  
Giovanni Floris
Keyword(s):  
Substrate Specificity ◽  
Amine Oxidase ◽  
Lentil Seedling

Oxidation of kynuramine by lentil seedling copper amine oxidase: demonstration of a single turnover mechanism in the apoenzyme

1998 ◽  
Vol 9 (5) ◽  
pp. 223-226 ◽  
Author(s):  
Alessandra Padiglia ◽  
Rosaria Medda ◽  
Anita Lorrai ◽  
Donatella Congiu ◽  
Jens Z. Pedersen ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Single Turnover ◽  
Lentil Seedling ◽  
Copper Amine

scholarly journals Tryptamine as Substrate and Inhibitor of Lentil Seedling Copper Amine Oxidase

1997 ◽  
Vol 250 (2) ◽  
pp. 377-382 ◽  
Author(s):  
Rosaria Medda ◽  
Alessandra Padiglia ◽  
Alessandro Finazzi Agro ◽  
Jens Z. Pedersen ◽  
Anita Lorrai ◽  
...  
Keyword(s):  
Amine Oxidase ◽  
Copper Amine Oxidase ◽  
Lentil Seedling ◽  
Copper Amine

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.

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