Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments.
J Biol Chem
; 259(21): 13172-7, 1984 Nov 10.
Article
en En
| MEDLINE
| ID: mdl-6490652
ABSTRACT
Mild acid hydrolysis of a small (Mr = 6 kDa) pectic polysaccharide isolated from tomato leaves, an inducer of the synthesis and accumulation of two proteinase inhibitors in excised tomato plants, yielded a alpha-D-polygalacturonic acid polymer with degree of polymerization = 20 that retained proteinase inhibitor-inducing activity. Enzymic and acid hydrolysis of this polygalacturonan yielded a series of alpha-1,4-D-galacturonic acid oligomers with degrees of polymerization from 2 to 6 which were purified to homogeneity and assayed for proteinase inhibitor-inducing activity in young excised tomato plants. All of the oligomers exhibited activity. The hexagalacturonide possessed the highest activity and the trimer the lowest. The evidence supports a possible role for plant cell wall fragments as systemic messengers that regulate the expression of proteinase inhibitor genes in plant leaves in response to pest attacks.
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Bases de datos:
MEDLINE
Asunto principal:
Plantas
/
Ácidos Urónicos
/
Pectinas
/
Ácidos Hexurónicos
Idioma:
En
Revista:
J Biol Chem
Año:
1984
Tipo del documento:
Article