ISSN:
1432-2242
Keywords:
Covalently bound wall proteins
;
Pollen
;
Pollen tubes
;
Tube growth
;
Incompatibility
;
Lily
;
Lilium longiforum
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
Notes:
Summary A method was worked out using trifluoromethanesulfonic acid (TFMS) as a reagent to split the covalently bound proteins, which are NaCl insoluble, from pollen tube walls of Lilium longiflorum, leaving the peptide bonds essentially intact. After electrophoretic separation, comparisons were made among these proteins from pollen grains and pollen tubes grown in vitro and in styles after self- and cross-pollination. It was found that a) the patterns of covalently bound wall proteins were different between tubes grown in vitro and in vivo; b) fewer bands were found in covalently bound wall proteins than that in noncovalently bound proteins; c) the bands remained almost the same no matter whether the tubes had been cross pollinated or self pollinated, indicating that while the noncovalently bound proteins were involved in incompatibility as shown in the previous paper, the covalently bound proteins may only serve as a structural component, having little to do with incompatibility.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00252065
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