Document Detail


Pollen-wall proteins: quantitative cytochemistry of the origins of intine and exine enzymes in Brassica oleracea.
MedLine Citation:
PMID:  972177     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Simultaneous coupling methods for detection of acid phosphatase and non-specific esterase produce a coloured reaction product that is quantitatively related to enzyme content in freeze-sectioned Brassica pollen and tapetal cells. The intine-located acid phosphatase has 2 periods of synthesis: the first in late vacuolate period, associated with the completion of deposition of the intine polysaccharides; the second during pollen maturation, apparently reflecting cytoplasmic synthesis, Esterase activity accumulates in the tapetal cells until dissolution at early maturation period, when there is a dramatic rise in pollen-wall esterase activity, reflecting the transfer from tapetum to exine cavities. These quantitative studies confirm the gametophytic and sporophytic origins of the intine and exine proteins.
Authors:
H I Vithanage; R B Knox
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of cell science     Volume:  21     ISSN:  0021-9533     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  1976 Jul 
Date Detail:
Created Date:  1976-12-03     Completed Date:  1976-12-03     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  423-35     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / biosynthesis,  metabolism*
Esterases / biosynthesis,  metabolism*
Histocytochemistry
Meiosis
Pollen / enzymology*,  ultrastructure
Vacuoles / ultrastructure
Chemical
Reg. No./Substance:
EC 3.1.-/Esterases; EC 3.1.3.2/Acid Phosphatase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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