Bedoukian   RussellIPM   RussellIPM   Piezoelectric Micro-Sprayer


Home
Animal Taxa
Plant Taxa
Semiochemicals
Floral Compounds
Semiochemical Detail
Semiochemicals & Taxa
Synthesis
Control
Invasive spp.
References

Abstract

Guide

Alphascents
Pherobio
InsectScience
E-Econex
Counterpart-Semiochemicals
Print
Email to a Friend
Kindly Donate for The Pherobase

« Previous AbstractMicrobial cycling of volatile organic sulfur compounds in anoxic environments    Next AbstractInduction of leucine aminopeptidase (LAP) like activity with wounding and methyl jasmonate in pigeonpea (Cajanas cajan) suggests the role of these enzymes in plant defense in leguminosae »

J Plant Physiol


Title:Changes and induction of aminopeptidase activities in response to pathogen infection during germination of pigeonpea (Cajanas cajan) seeds
Author(s):Lomate PR; Hivrale VK;
Address:"Department of Biochemistry, Dr. Babasaheb Ambedkar Marathwada University, Aurangabad 431004, Maharashtra, India"
Journal Title:J Plant Physiol
Year:2011
Volume:168
Issue:15
Page Number:1735 - 1742
DOI: 10.1016/j.jplph.2011.05.002
ISSN/ISBN:1618-1328 (Electronic) 0176-1617 (Linking)
Abstract:"Aminopeptidases play important role in the mobilization of storage proteins at the cotyledon during seed germination. It is often referred as inducible component of defense against herbivore attack. However the role of aminopeptidase in response to pathogen attack in germinating seeds is remained to be unknown. An attempt was made to analyze change in the aminopeptidase (EC 3.4.11.1) activity during germination of pigeonpea (Cajanus cajan L.) seeds by infecting the seeds with fungi. Two aminopeptidase activity bands (AP1 and AP2) were detected in control as well as infected pigeonpea seeds. During latter stages of germination in control seeds, AP1 activity was replaced by AP2 activity. However AP1 activity was significantly induced in germinating seeds infected with Fusarium oxysporum f.sp. ciceri and Aspergillus niger var. niger. The estimated molecular weights of AP1 and AP2 were approximately 97 and 42.8kDa respectively. The induced enzyme was purified up to 30 fold by gel filtration chromatography. The purified enzyme was preferentially cleaved leucine p-nitroanilide than alanine p-nitroanilide. The enzyme was strongly inhibited by bestatin and 1,10-phenanthroline. Almost 50% of enzyme activity was inhibited by ethylene diamine tetra acetate. The purified enzyme showed broad pH optima ranging from pH 6.0 to 9.0 and optimum at pH 8.5. The induction of aminopeptidase activity during pigeonpea seed germination and in response to pathogen attack indicates significant involvement of these enzymes in primary as well as secondary metabolism of the seeds. These findings could be helpful to further dissect defensive role of aminopeptidases in seed germination which is an important event in plant's life"
Keywords:"Aminopeptidases/antagonists & inhibitors/chemistry/isolation & purification/*metabolism Aspergillus niger/*physiology Cajanus/*enzymology/growth & development/microbiology/physiology Chromatography, Gel Edetic Acid/pharmacology Fusarium/*physiology Germin;"
Notes:"MedlineLomate, Purushottam R Hivrale, Vandana K eng Research Support, Non-U.S. Gov't Germany 2011/06/07 J Plant Physiol. 2011 Oct 15; 168(15):1735-42. doi: 10.1016/j.jplph.2011.05.002"

 
Back to top
 
Citation: El-Sayed AM 2024. The Pherobase: Database of Pheromones and Semiochemicals. <http://www.pherobase.com>.
© 2003-2024 The Pherobase - Extensive Database of Pheromones and Semiochemicals. Ashraf M. El-Sayed.
Page created on 22-11-2024