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The use of immunological methods to study the activity of cellulase isozymes (B 1:4 glucan 4‐glucan hydrolase) in bean leaf abscission
Author(s) -
DURBIN M. L.,
SEXTON R.,
LEWIS L. N.
Publication year - 1981
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.1981.tb00836.x
Subject(s) - abscission , cellulase , isozyme , phaseolus , glucan , biology , enzyme , biochemistry , enzyme assay , botany , chemistry
The changes in the levels of two different isozymes of cellulase (EC 3.2.1.4) have been followed during the abscission of the primary leaves of bean ( Phaseolus vulgaris c.v. Red Kidney), using antibodies raised against the 9.5 form of the enzyme. Data from both radioimmune and direct assay show that the 9.5 form of cellulase is undetectable prior to the induction of abscission. After a 12 h lag this isozyme increases in activity, the increase preceding a decrease in integrity of the abscission zone cell walls. The results are consistent not only with the view that this specific isozyme is involved in wall hydrolysis but also with previous data which showed that cellulase is synthesized ‘de novo’. The 4.5 isozyme of cellulase is more widely spread throughout the plant, being most active in young tissues. During abscission the activity of this isozyme in the abscission layer falls and consequently it is not thought to be involved directly in the abscission process.