scholarly journals Participation of Chitin-Binding Peroxidase Isoforms in the Wilt Pathogenesis of Cotton

2011 ◽  
Vol 02 (01) ◽  
pp. 43-49 ◽  
Author(s):  
Egor Pshenichnov ◽  
Nigora Khashimova ◽  
Alik Akhunov ◽  
Zamira Golubenko ◽  
Robert D. Stipanovic
Keyword(s):  
2001 ◽  
Vol 52 (354) ◽  
pp. 25-35 ◽  
Author(s):  
Annamaria Ranieri ◽  
Antonella Castagna ◽  
Barbara Baldan ◽  
Gian Franco Soldatini

2002 ◽  
Vol 14 (3) ◽  
pp. 219-224 ◽  
Author(s):  
Isabel Regina Prazeres de Souza ◽  
Vera Maria Carvalho Alves ◽  
Sidney Netto Parentoni ◽  
Antônio Carlos de Oliveira ◽  
Flávia França Teixeira ◽  
...  

The effects of a short-term (80 min) exposure to 222 µM aluminum (Al) on the protein content and expression and on peroxidase activity and isoenzymes in the primary root of maize were evaluated. Two inbred lines differing in their level of tolerance to Al were used: Cateto 237 (tolerant) and L36 (sensitive). The apical 20 mm of the primary root was divided into 2-mm-long segments that were analyzed for total protein content and peroxidase activity. These results demonstrate that the total protein content along the root apex was not affected by Al in the tolerant inbred line, but decreased in the sensitive line. In the apical 2 mm of the root of the sensitive line, the expression of low molecular weight proteins (43 kDa or smaller) was decreased. Expression of low molecular proteins increased in the tolerant inbred line, even though total protein content did not increase. This suggests that some of these proteins could play a role in metal tolerance, perhaps as binding peptides. While the peroxidase activity of the tolerant inbred line did not change with exposure to Al, peroxidase activity in the apical 6 mm of the root of the sensitive line decreased. The tolerant inbred line constitutively expressed more anionic peroxidase isoforms. These results demonstrate that maintenance of protein expression may be an important component of the plant's resistance to Al stress, and that resistance to Al stress is associated with the higher expression of anionic peroxidase isoforms.


2001 ◽  
Vol 52 (354) ◽  
pp. 25-35 ◽  
Author(s):  
Annamaria Ranieri ◽  
Antonella Castagna ◽  
Barbara Baldan ◽  
Gian Franco Soldatini

LWT ◽  
1997 ◽  
Vol 30 (2) ◽  
pp. 192-201 ◽  
Author(s):  
Stewart Boyes ◽  
Paul Chevis ◽  
Conrad Perera

2006 ◽  
Vol 281 (28) ◽  
pp. 19655-19664 ◽  
Author(s):  
Astrid Borchert ◽  
Chi Chiu Wang ◽  
Christoph Ufer ◽  
Heike Schiebel ◽  
Nicolai E. Savaskan ◽  
...  

HortScience ◽  
2005 ◽  
Vol 40 (3) ◽  
pp. 546-548
Author(s):  
Suping Zhou ◽  
Roger J. Sauvé ◽  
Margaret T. Mmbaga ◽  
Chaim Frenkel

Leucanthemum maximum `Silver Princess' plants, that were gradually acclimated for 7 days at 10 °C followed by 28 days at 7 °C, were subjected to the following cold treatments: 30 days at 4 °C; 4 or 5 days at 0 °C and for 3 hours at –1 °C to identify cold inducible proteins that may be responsible for cold tolerance in this cold tolerant species. Change in antioxidant enzymes activity in fully expanded leaves was assessed after each treatment. Catalase activity began to increase after 30 days at 4 °C and reached its peak after a 5-day exposure to 0 °C. The activity of cellular glutathione peroxidase and glutathione reductase significantly increased after a 4-day exposure to 0 °C. Changes in activity of four active superoxide dismutase isoforms, one basic guaiacol peroxidase and two o-dianisine peroxidase isoforms were also detected following the full series of cold treatments (30 days at 4 °C; 4 or 5 days at 0 °C and for 3 hours at –1 °C).


2000 ◽  
Vol 156 (2) ◽  
pp. 266-271 ◽  
Author(s):  
Annamaria Ranieri ◽  
Antonella Castagna ◽  
Gian Franco Soldatini

2015 ◽  
Vol 338 (12) ◽  
pp. 793-802 ◽  
Author(s):  
Marija Petrić ◽  
Angelina Subotić ◽  
Slađana Jevremović ◽  
Milana Trifunović-Momčilov ◽  
Vojin Tadić ◽  
...  
Keyword(s):  

2003 ◽  
Vol 105 (3) ◽  
pp. 300-304 ◽  
Author(s):  
Hubert Mörk ◽  
Michael Scheurlen ◽  
Oliver Al-Taie ◽  
Annette Zierer ◽  
Michael Kraus ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document