Abstract

This paper reports results of two-dimensional gel electrophoresis analysis of pollen coat and pollen protoplast proteins of self-incompatible and self-fertile Secale cereale as well as pollen collected from Festuca pratensis populations and selected self-sterile plants. Washing pollen 10 times in isotonic buffer showed that the first and second fractions contained the majority of the pollen coat proteins. Results of protein analysis are discussed against the background of pollen wall ultrastructure. A fraction of peptides found in the pollen coat were also present in the protein patterns of protoplasts; however, numerous pollen coat peptides were not detected in the protoplast and vice versa. The self-incompatible S. cereale had 23 pollen coat peptides and 46 from protoplasts that differed in molecular weight (MW) and isoelectric point (IP) in comparison to those of pollen coat and protoplasts of self-fertile S. cereale. Similarly, self-sterile F. pratensis had 60 pollen coat peptides and 11 protoplast peptides different from those of the self-sterile/self-fertile F. pratensis. The pollen coat fraction of the self-incompatible S. cereale and the self-sterile plants of F. pratensis had three peptides with very similar MW and IP, whereas in their protoplasts two peptides with similar MW and IP were found. The possible relationship between pollen ultrastructural organisation and rate of protein elution is discussed.

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