Purification of amine oxidase from Pisum sativum for the construction of amine biosensors

2004 ◽  
Vol 53 (4) ◽  
pp. 165
Author(s):  
T Rinken ◽  
A Vaarik
Keyword(s):  
Pisum Sativum ◽  
Amine Oxidase

scholarly journals Activities of amine oxidase, peroxidase and catalase in seedlings of Pisum sativum L. under different light conditions

2011 ◽  
Vol 49 (No. 4) ◽  
pp. 151-157 ◽  
Author(s):  
L. Luhová ◽  
A. Lebeda ◽  
D. Hedererová ◽  
P. Peč
Keyword(s):  
Pisum Sativum ◽  
Enzyme Activities ◽  
Oxidase Activity ◽  
Amine Oxidase ◽  
Field Pea ◽  
Light Conditions ◽  
Green Plants ◽  
Pisum Sativum L ◽  
Etiolated Plants ◽  
Amine Oxidase Activity

The activities of amine oxidase, peroxidase and catalase were studied in 12 cultivars of field pea (Pisum sativum L.) and one accession of wild pea (Pisum sativum subsp. transcaucasicum). The influence of different light conditions on the enzyme activities was studied in extracts of 8-d-old seedlings. Substantially higher amine oxidase activity was detected in etiolated pea seedlings than in plants growing under controlled light conditions (12h photoperiod). Higher peroxidase and catalase activities indicate more intensive production of toxic hydrogen peroxide evolved by reactions of different type in green plants in comparison with etiolated ones. Significantly lower activity of peroxidases in etiolated plants could be related to a lower degree of lignification. Marked differences in enzyme activities between etiolated field pea and P. sativum subsp. transcaucasicum were observed for all studied enzymes. A very interesting result was the exceptionally low activity of amine oxidase in etiolated plants that was hardly detectable in green plants of Malton cultivar. Two bands with amine oxidase activity were found by the method of native PAGE in extracts of 8-d-old plants. A different relationship of these isoenzymes was detected in field pea and wild pea. Two isoenzymes were present in pea shoots but only one isoenzyme was detected in pea roots. Amine oxidase isoenzymes were studied in the roots and shoots of cv. Smaragd for three weeks. The profile of isoenzymes was opposite in 8- and 36-d-old stems of pea.

scholarly journals Purification and Properties of Amine Oxidase from Epicotyls of Pisum sativum

1971 ◽  
Vol 47 (5) ◽  
pp. 644-648 ◽  
Author(s):  
Roy E. McGowan ◽  
Robert M. Muir
Keyword(s):  
Pisum Sativum ◽  
Amine Oxidase ◽  
Purification And Properties

A proposed interplay between peroxidase, amine oxidase and lipoxygenase in the wounding-induced oxidative burst in Pisum sativum seedlings

2015 ◽  
Vol 112 ◽  
pp. 130-138 ◽  
Author(s):  
Thomas Roach ◽  
Louise Colville ◽  
Richard P. Beckett ◽  
Farida V. Minibayeva ◽  
Michel Havaux ◽  
...  
Keyword(s):  
Pisum Sativum ◽  
Oxidative Burst ◽  
Amine Oxidase

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.

Sign in / Sign up

Export Citation Format

Share Document