Partial Purification and Characterization of a Glycoprotein Cell Fusion Hormone from Griffithsia pacifica, a Red Alga
Author(s) -
Bruce A. Watson,
Susan D. Waaland
Publication year - 1983
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.71.2.327
Subject(s) - concanavalin a , glycoprotein , size exclusion chromatography , cell fusion , affinity chromatography , biology , cell , biochemistry , cell division , chemistry , chromatography , in vitro , enzyme
In filaments of the red alga Griffithsia, dead intercalary cells are replaced by the process of cell repair by cell fusion. This process is coordinated by a morphogenetic cell fusion hormone, rhodomorphin, which accelerates cell division and induces the production of a specialized repair cell. We have isolated rhodomorphin from Griffithsia pacifica Kylin and have purified it by concanavalin A affinity chromatography, hydrophobic interaction chromatography, and gel filtration chromatography. This molecule binds specifically to concanavalin A, is proteinase sensitive, and is inactivated by short treatments at temperatures of 50 degrees C or above. It therefore appears that rhodomorphin from G. pacifica is a glycoprotein; its molecular weight, as estimated by gel filtration, is approximately 14,000.
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