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Purification and immunolocalization of an annexin-like protein in pea seedlingsAs part of a study to identify potential targets of calcium action in plant cells, a 35-kDa, annexin-like protein was purified from pea (Pisum sativum L.) plumules by a method used to purify animal annexins. This protein, called p35, binds to a phosphatidylserine affinity column in a calcium-dependent manner and binds 45Ca2+ in a dot-blot assay. Preliminary sequence data confirm a relationship for p35 with the annexin family of proteins. Polyclonal antibodies have been raised which recognize p35 in Western and dot blots. Immunofluorescence and immunogold techniques were used to study the distribution and subcellular localization of p35 in pea plumules and roots. The highest levels of immunostain were found in young developing vascular cells producing wall thickenings and in peripheral root-cap cells releasing slime. This localization in cells which are actively involved in secretion is of interest because one function suggested for the animal annexins is involvement in the mediation of exocytosis.
Document ID
Document Type
Reprint (Version printed in journal)
External Source(s)
Clark, G. B. (University of Texas Austin 78713, United States)
Dauwalder, M.
Roux, S. J.
Date Acquired
August 21, 2013
Publication Date
January 1, 1992
Publication Information
Publication: Planta
Volume: 187
ISSN: 0032-0935
Subject Category
Life Sciences (General)
Funding Number(s)
CONTRACT_GRANT: 1-T32-HD07296-01A3
Distribution Limits
NASA Discipline Number 40-50
NASA Discipline Plant Biology
NASA Program Space Biology
Non-NASA Center