Abstract

In the host pathogen interaction between Pisum sativum and Pseudomonas syringae pv. pisi the levels of the two enzymes s 1,3 glucanase and chitinase change after infection. In three pea cultivars examined: Fortune PS 890751, Kelvedon Wonder PS 91029 and Early Onward PS 89074, the levels of the two enzymes increased in intercellular fluids (IF) after infection with race 1 (299A) and race 2 (202) of the pathogen when compared with the healthy plant. The s1,3 glucanase activity was found in three isozymes with isoelectric points of 9.0, 7.8 and 4.6 in Fortune (F) and Kelvedon Wonder (K). The differential cultivar Early Onward (E) which shows hypersensitivity when infected with race 2 of the pathogen and susceptibility when infected with race 1 has four s1, 3 giucanases of isoelectric points 9.0, 8.4, 7.8 and 4.6. Western blotting of intercellular fluids and acidic (pH 2.3) and basic (pH 8.3) extracts showed that Fortune produced a 21 kDa protein which was detected by the s1,3 glucanase and the chitinase/lysozyme antisera.This 21 kDa protein was present both in the susceptible reaction (Fortune x R6) and the resistant reaction (Fortune x R1, Fortune x R 2). In the Early Onward resistant reaction (Early Onward x R2) and the susceptible interaction (Early Onward x R1, Early Onward x R6) a 29 kDa protein was detected by the s1,3 glucanase antisera and the chitinase/lysozyme antisera in the intercellular fluids and the acidic and basic extracts. The universally susceptible cultivar Kelvedon Wonder produced a protein of the same molecular weight (29 kDa) as Early Onward along with another protein of 33kDa detected by the chitinase/lysozyme antisera.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.