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Binding of plant isoperoxidases to pectin in the presence of calcium
Author(s) -
Penel Claude,
Greppin Hubert
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80605-5
Subject(s) - pectin , chemistry , polysaccharide , biochemistry , pectinesterase , centrifugation , size exclusion chromatography , cationic polymerization , calcium , chromatography , enzyme , organic chemistry , pectinase
Some of the isoperoxidases present in an extract from zucchini hypocotyls ‐ one anionic and two cationic ‐ exhibited a Ca 2+ ‐dependent pelletability which resulted from an interaction with pectins. Endogenous pectins could be replaced by polygalacturonic acid or pectin extracted from citrus, but not by highly esterifled pectin. The interaction between the isoperoxidases and the polysaccharides has been studied by centrifugation, by gel filtration, and with pectins attached in wells of a microtitration plate. These various binding tests have shown that the isoperoxidases had an affinity for the pectins in their Ca 2+ ‐induced conformation.