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PECTINASE IN ASCLEPIAS LATEX AND ITS POSSIBLE ROLE IN LATICIFER GROWTH AND DEVELOPMENT
Author(s) -
Wilson Kathryn J.,
Nessler Craig L.,
Mahlberg Paul G.
Publication year - 1976
Publication title -
american journal of botany
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.218
H-Index - 151
eISSN - 1537-2197
pISSN - 0002-9122
DOI - 10.1002/j.1537-2197.1976.tb13199.x
Subject(s) - pectinase , pectin , biology , middle lamella , enzyme , ammonium sulfate , chromatography , biochemistry , chemistry , cell wall
A pectinase with a p H optimum of 5.2 is present in the latex of the common milkweed, Asclepias syriaca L. The enzyme was partially purified from the serum fraction of fresh latex by dialysis and ammonium sulfate fractionation. Enzyme activity was detected by a viscometry assay and by the dinitrosalicylic acid assay for reducing sugars. Pectin and polygalacturonic acid could serve as substrates for the enzyme. Pectolytic activity in latex presents a basis for describing the development of the non‐articulated branched laticifer system. Enzyme activity may facilitate intrusive tip growth of the laticifer among other cells by solubilizing pectic substances of the middle lamella and also may be important for loosening wall material of the laticifer itself to facilitate extension growth.