Self-incompatibility alleles control a low molecular weight, basic protein in pistils of Petunia hybrida
- 1 March 1986
- journal article
- research article
- Published by Springer Nature in Theoretical and Applied Genetics
- Vol. 71 (6), 815-819
- https://doi.org/10.1007/bf00276423
Abstract
Proteins extracted from the pistils of several clones of Petunia hybrida carrying differing pairs of S alleles were examined by gel electrophoresis. The major protein of pistils, a basic glycoprotein of relatively low molecular weight, showed properties which varied in a simple manner with the S genotype. For each S allele we were able to assign a specific molecular weight (ranging from 27,000 to 33,000) and isoelectric point (in the range 8.3 to 8.7) for this putative S protein. Pistils homozygous at the S locus showed only one major protein on two-dimensional gel electrophoresis, while pistils from plants heterozygous at the S locus showed two. No evidence was obtained for the presence of this putative S protein in pollen extracts.Keywords
This publication has 16 references indexed in Scilit:
- Pollen—Pistil Recognition: New Concepts from Electron Microscopy and CytochemistryInternational Review of Cytology, 1984
- Review Lecture Self-incompatibility: phenomenology and physiologyProceedings of the Royal Society of London. B. Biological Sciences, 1983
- Localization of phytic acid in the floral structure of Petunia hybrida and relation to the incompatibility genesTheoretical and Applied Genetics, 1983
- Isolation and partial characterization of components of Prunus avium L. styles, including an antigenic glycoprotein associated with a self-incompatibility genotypePlanta, 1982
- S-specific proteins in styles of self-incompatible Nicotiana alataTheoretical and Applied Genetics, 1981
- Incompatibility in PetuniaProceedings of the Royal Society of London. B. Biological Sciences, 1975
- Maturation of the head of bacteriophage T4Journal of Molecular Biology, 1973
- [5] Molecular weight determination of glycoproteins by polyacrylamide gel electrophoresis in sodium dodecyl sulfateMethods in Enzymology, 1972
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Serological reactions of pollen incompatibility substancesProceedings of the Royal Society of London. B. Biological Sciences, 1952