Pollen-wall proteins: quantitative cytochemistry of the origins of intine and exine enzymes in Brassica oleracea.
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.
D000135:Acid Phosphatase / Q000096:biosynthesis / Q000378:metabolism*; D004950:Esterases / Q000096:biosynthesis / Q000378:metabolism*; D006651:Histocytochemistry; D008540:Meiosis; D011058:Pollen / Q000201:enzymology* / Q000648:ultrastructure; D014617:Vacuoles / Q000648:ultrastructure
D004950:Esterases; D000135:Acid Phosphatase